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Arginase Deficiency

Synonym: Hyperargininemia

, MD, , MD, and , MD.

Author Information

Initial Posting: ; Last Update: August 28, 2014.

Estimated reading time: 15 minutes


Clinical characteristics.

Arginase deficiency in untreated individuals is characterized by episodic hyperammonemia of variable degree that is infrequently severe enough to be life threatening or to cause death. Most commonly, birth and early childhood are normal. Untreated individuals have slowing of linear growth at age one to three years, followed by development of spasticity, plateauing of cognitive development, and subsequent loss of developmental milestones. If untreated, arginase deficiency usually progresses to severe spasticity, loss of ambulation, complete loss of bowel and bladder control, and severe intellectual disability. Seizures are common and are usually controlled easily.


Many if not most affected infants will be identified by the current full-panel expanded newborn screening testing done in many states and countries. Three- to fourfold elevation of plasma arginine concentration above the upper limit of normal is highly suggestive of the diagnosis. The diagnosis is confirmed by identification of biallelic ARG1 pathogenic variants on molecular genetic testing or failure to detect arginase enzyme activity (usually <1% of normal) in red blood cell extracts.


Treatment of manifestations: Management should closely mirror that for urea cycle disorders, except that individuals with arginase deficiency are unlikely to have episodes of hyperammonemia; if present, such episodes are likely to respond to conservative management (e.g., intravenous fluid administration). Treatment should be by a team coordinated by a metabolic specialist. Treatment of an acutely ill (comatose and encephalopathic) individual requires rapid reduction of plasma ammonia concentration, use of pharmacologic agents (sodium benzoate and/or sodium phenylbutyrate/phenylacetate) to allow excretion of excess nitrogen through alternative pathways, introduction of calories supplied by carbohydrates and fat to reduce catabolism and the amount of excess nitrogen in the diet, and physiologic stabilization with intravenous fluids and cardiac pressors as necessary while avoiding overhydration and resulting cerebral edema.

Prevention of primary manifestations: Maintenance of plasma arginine concentration as near normal as possible through restriction of dietary protein and use of oral nitrogen-scavenging drugs.

Surveillance: Regular follow-up at intervals determined by age and degree of metabolic stability.

Agents/circumstances to avoid: Valproic acid (exacerbates hyperammonemia).

Evaluation of relatives at risk: Plasma quantitative amino acid analysis, molecular genetic testing (if the family-specific pathogenic variants are known), or enzymatic testing in all sibs (especially younger ones) of a proband to allow early diagnosis and treatment of those found to be affected.

Other: Prompt treatment of acute intercurrent illnesses with special dietary intervention or hospitalization to minimize the effect of catabolism.

Genetic counseling.

Arginase deficiency is inherited in an autosomal recessive manner. At conception, each sib of an affected individual has a 25% chance of being affected, a 50% chance of being an asymptomatic carrier, and a 25% chance of being unaffected and not a carrier. Heterozygotes (carriers) are asymptomatic. Carrier testing for at-risk relatives and prenatal testing for pregnancies at increased risk are possible if the ARG1 pathogenic variants in the family are known.


Suggestive Findings

Arginase deficiency should be suspected in either of the following:

  • Newborns with elevation of arginine on the current full-panel expanded newborn screening testing done in many states and countries
  • Individuals with progressive loss of developmental milestones and spasticity

Preliminary Testing

Plasma quantitative amino acid analysis. Elevation of plasma arginine concentration three- to fourfold above the upper limit of normal is highly suggestive of the diagnosis. Plasma arginine elevation is the primary means of ascertainment.

Note: Up to twofold elevations may be seen in infants who do not have arginase deficiency and who are otherwise normal.

Plasma ammonia concentration. Elevation of plasma ammonia concentration may be intermittent. Acute hyperammonemia (plasma ammonia concentration >150 µmol/L) is uncommon.

Urinary orotic acid concentration. Although urinary orotic acid concentration is often elevated, it is not a primary screen for the disorder.

Establishing the Diagnosis

The diagnosis of arginase deficiency is established in a proband with either biallelic pathogenic variants in ARG1 (see Table 1) or reduced red blood cell arginase enzyme activity.

Note: Until recently, red blood cell arginase enzyme testing was the gold standard for diagnostic confirmation; however, molecular genetic testing is now readily available and is an alternative to enzyme testing as the first-line confirmatory test. Enzyme assay remains the norm if two pathogenic variants are not found.

Molecular genetic testing

  • One molecular genetic testing strategy is sequence analysis of ARG1 followed by deletion/duplication analysis if both ARG1 pathogenic variants are not identified on sequence analysis.
  • An alternative molecular genetic testing strategy is use of a multigene panel that includes ARG1 and other genes of interest (see Differential Diagnosis). Note: (1) The genes included in the panel and the diagnostic sensitivity of the testing used for each gene vary by laboratory and are likely to change over time. (2) Some multigene panels may include genes not associated with the condition discussed in this GeneReview; thus, clinicians need to determine which multigene panel is most likely to identify the genetic cause of the condition at the most reasonable cost while limiting identification of variants of uncertain significance and pathogenic variants in genes that do not explain the underlying phenotype. (3) In some laboratories, panel options may include a custom laboratory-designed panel and/or custom phenotype-focused exome analysis that includes genes specified by the clinician. (4) Methods used in a panel may include sequence analysis, deletion/duplication analysis, and/or other non-sequencing-based tests.
    For an introduction to multigene panels click here. More detailed information for clinicians ordering genetic tests can be found here.

Table 1.

Molecular Genetic Testing Used in Arginase Deficiency

Gene 1Test MethodProportion of Probands with a Pathogenic Variant Detectable by This Method
ARG1Sequence analysis 2See footnote 3
Deletion/duplication analysis 4See footnote 5

See Table A. Genes and Databases for chromosome locus and protein. See Molecular Genetics for information on allelic variants detected in this gene.


Sequence analysis detects variants that are benign, likely benign, of uncertain significance, likely pathogenic, or pathogenic. Pathogenic variants may include small intragenic deletions/insertions and missense, nonsense, and splice site variants; typically, exon or whole-gene deletions/duplications are not detected. For issues to consider in interpretation of sequence analysis results, click here.


Sequence analysis of the ARG1 coding region has detected pathogenic variants in most affected individuals tested to date, but sample size is small and no statement about variant detection rate can be made at this time [J Haberle, personal communication].


Testing that identifies exon or whole-gene deletions/duplications not detectable by sequence analysis of the coding and flanking intronic regions of genomic DNA. Included in the variety of methods that may be used are: quantitative PCR, long-range PCR, multiplex ligation-dependent probe amplification (MLPA), and chromosomal microarray (CMA) that includes this gene/chromosome segment.


Whole-gene deletion, beginning in intron 1 and including the remainder of the gene, has been reported [Korman et al 2004]

Measurement of red blood cell arginase enzyme activity. Most affected individuals have no detectable arginase enzyme activity (usually <1% of normal) in red blood cell extracts.

Note: (1) Although arginase is stable, a control sample should be obtained and treated identically if the cells are to be shipped to a distant site. (2) Arginase enzyme activity is reduced in liver as well as red blood cells, but arginase enzyme activity in liver is rarely measured because of the risks involved in liver biopsy and the ease of diagnosis from red blood cells.

Clinical Characteristics

Clinical Description

Unlike any of the other eight primary urea cycle disorders (see Urea Cycle Disorders Overview), arginase deficiency rarely results in elevated plasma ammonia concentration in the newborn period, even in individuals with two null variants. Episodic hyperammonemia of variable degree may occur but is rarely severe enough to be life threatening or to cause death. Hyperammonemia is often recognized only if blood ammonia or plasma amino acid concentrations are obtained during an acute illness. Although data are not available, it appears that more than 75% of affected individuals survive their disease and live long, albeit handicapped lives.

Most commonly, birth and early childhood are normal. At the age of one to three years, linear growth slows and spasticity, more commonly spastic diplegia, begins to develop. Soon, previously normal cognitive development slows or stops and the child begins to lose developmental milestones. If untreated, arginase deficiency usually progresses to severe spasticity, loss of ambulation, complete loss of bowel and bladder control, and severe intellectual disability.

Some children are more severely affected cognitively, whereas others have more severe spasticity and secondary joint contractures.

All affected individuals have growth deficiency.

Seizures are common and are usually controlled easily.

Microcephaly is common and brain imaging often reveals cortical atrophy.

Other parts of the nervous system including basal ganglia, cerebellum, medulla, and spinal cord are largely spared [De Deyn et al 1997].

Older individuals may present with postoperative encephalopathy.

Genotype-Phenotype Correlations

No genotype-phenotype correlations have been described.

The degree of enzyme deficiency in red blood cells or the genotype cannot be used to establish disease severity or prognosis as they are but two of several factors involved in the outcome.


Arginase deficiency is thought to be one of the least common of the urea cycle defects. Its incidence has been estimated at between 1:350,000 and 1:1,000,000; the true incidence in non-related populations is unknown.

Arginase deficiency may be more common in parts of Japan and among French Canadians.

Differential Diagnosis

Hyperammonemia. Arginase is the sixth and final enzyme of the eight known steps in the urea cycle. See Urea Cycle Disorders Overview for approaches to distinguish:

  • Other causes of hyperammonemia from a urea cycle disorder; and
  • The differences between the urea cycle disorders themselves.

Spasticity. Arginase deficiency may be misdiagnosed as static spastic diplegia (cerebral palsy). It should be noted that arginase deficiency is one of the few treatable causes of spastic diplegia [Prasad et al 1997].

ARG2. A second arginase gene is known (ARG2), but no human deficiency state has been identified and it is not clear that elevated plasma arginine would be a part of such a deficiency.


Evaluations Following Initial Diagnosis

To establish the extent of disease and needs in an individual diagnosed with arginase deficiency, the following evaluations are recommended:

  • Plasma ammonia concentration
  • Plasma arginine concentration
  • Developmental assessment
  • Complete neurologic evaluation
  • Consultation with a clinical geneticist and/or genetic counselor

Treatment of Manifestations

The management of individuals with arginase deficiency should closely mirror that described in the Urea Cycle Disorders Overview, with one caveat: individuals with arginase deficiency are less prone to episodes of hyperammonemia and when present, hyperammonemia is more likely to respond to conservative management such as intravenous fluid administration. However, the individual who is comatose and encephalopathic is at high risk for severe brain damage and should be treated accordingly. Arginine supplementation is obviously contraindicated.

Infants should be managed by a team coordinated by a metabolic specialist in a specialized center. In the acute phase, the mainstays of treatment are the following:

  • Rapidly reducing plasma ammonia concentration. The best way to reduce plasma ammonia concentration quickly is by dialysis; the faster the flow rate of dialysate, the faster the clearance of ammonia from the plasma. The method employed depends on the affected individual's circumstances and available resources. Fastest is use of pump-driven dialysis, in which an extracorporeal membrane oxygenation (ECMO) pump is used to drive a hemodialysis (HD) machine. Other methods are "routine" hemodialysis, hemofiltration (both arteriovenous and venovenous), peritoneal dialysis, and continuous-drainage peritoneal dialysis. Dialysis can usually be discontinued when plasma ammonia concentration falls below 200 µmol/L. Affected individuals often experience a "rebound" hyperammonemia that may require further dialysis, although rarely is this level of intervention required in arginase deficiency.
  • Pharmacologic management to allow alternative pathway excretion of excess nitrogen. Blocking of ammonia production and the need for ureagenesis is accomplished by diminishing catabolism with adequate non-protein calories and with a combination of the nitrogen scavenger drugs sodium phenylacetate and sodium benzoate. A loading dose of the drugs is followed by maintenance administration, initially intravenously and later orally when the individual is stable. Intravenous forms of these medications are now approved by the FDA and are generally available.
  • Reducing the amount of excess nitrogen in the diet and reducing catabolism through the introduction of calories supplied by carbohydrates and fat. In acutely ill individuals, calories should be provided as carbohydrate and fat, either intravenously as glucose and Intralipid® or orally as protein-free oral formula, such as Mead Johnson 80056® or Ross Formula ProPhree®; however, complete restriction of protein should not exceed 24-48 hours, as depletion of essential amino acids may result in endogenous protein catabolism and nitrogen release. High parenteral glucose plus insulin can be used acutely to diminish endogenous protein catabolism. Individuals should be transitioned from parenteral to enteral feeds as soon as possible. In early treatment, feeding 1.0 to 1.5 g of protein/kg body weight with 50% as essential amino acids is advised, particularly for infants. Older children require and tolerate lower protein intake.
  • Reducing the risk of neurologic damage. Cautionary measures are physiologic stabilization with intravenous fluids (10% dextrose with one-quarter normal saline) and cardiac pressors as necessary while avoiding overhydration and resulting cerebral edema, the duration of which correlates with poor neurologic outcome.

Older individuals are at risk for episodes of hyperammonemia and should continue to be managed by a specialist in metabolic disorders.

Seizures are easily treated by phenobarbital or carbamazepine.

Acute intercurrent illnesses should be treated promptly with special dietary intervention or hospitalization to minimize the effect of catabolism.

Prevention of Primary Manifestations

The goal should be maintenance of plasma arginine concentration as near normal as possible, consistent with the individual's tolerance for the following interventions:

  • Restriction of dietary protein through use of specialized formulas. In the best of circumstances, the affected individual should be on the minimal protein intake needed to maintain protein biosynthetic function, growth, and normal or near-normal plasma amino acid concentrations. Half or more of dietary protein should be an arginine-free essential amino acid mixture.
  • Administration of oral nitrogen scavenging drugs. Sodium phenylbutyrate/glycerolphenylbutyrate at a dose of 350-600 mg/kg/day in patients weighing less than 20 kg, or 9.9-13.0 g/m2/day in larger patients. The medicines are to be taken in equally divided amounts with each meal or feeding (i.e., 3-6x/day) [De Deyn et al 1997, Iyer et al 1998, Urea Cycle Disorders Consortium].
  • Liver transplantation eliminates the hyperargininemia and presumably the risk for hyperammonemia.

Prevention of Secondary Complications

Most individuals with arginase deficiency have persistent hepatic synthetic function abnormalities; particularly, elevated prothrombin time.

In some circumstances hepatic fibrosis and cirrhosis have developed and have either been fatal or required a liver transplant.

Arginine is the substrate for nitric oxide synthase; however, abnormalities in this pathway have not been described.

The spasticity may be reactive and instances of marked improvement with Botox® have been described.


Patients are seen at regular intervals determined by their age and degree of metabolic stability.

Infants should be seen monthly or more frequently, with monitoring of plasma concentration of ammonia and amino acids, growth, and neurologic function. If treatment fails to arrest the neurologic deterioration or if spasticity is symptomatic, appropriate orthopedic and physical therapy interventions are indicated.

Agents/Circumstances to Avoid

Valproic acid is to be avoided as it exacerbates hyperammonemia in urea cycle defects and other inborn errors of metabolism [Scaglia & Lee 2006].

Evaluation of Relatives at Risk

Because the age of onset of arginase deficiency is delayed beyond the newborn period and the manifestations can vary, the genetic status of all sibs of a proband (especially the younger ones) should be clarified so that morbidity can be reduced by early diagnosis and treatment in those who are affected. Testing methods can include any one of the following:

  • Plasma quantitative amino acid analysis
  • Molecular genetic testing (if the family-specific ARG1 pathogenic variants are known)
  • Analysis of enzymatic activity in red blood cells

See Genetic Counseling for issues related to testing of at-risk relatives for genetic counseling purposes.

Pregnancy Management

The authors are not aware of any instance in which pregnancy has been reported in a woman with arginase deficiency; therefore, no inference can be drawn about the safety of pregnancy for the mother or the fetus.

Therapies Under Investigation

Search in the US and in Europe for access to information on clinical studies for a wide range of diseases and conditions. Note: There may not be clinical trials for this disorder.


Immunizations can be provided on the usual schedule.

Multivitamin and fluoride supplementation are indicated for all affected individuals.

Appropriate use of antipyretics is indicated. Ibuprofen is preferred over acetaminophen.

Genetic Counseling

Genetic counseling is the process of providing individuals and families with information on the nature, inheritance, and implications of genetic disorders to help them make informed medical and personal decisions. The following section deals with genetic risk assessment and the use of family history and genetic testing to clarify genetic status for family members. This section is not meant to address all personal, cultural, or ethical issues that individuals may face or to substitute for consultation with a genetics professional. —ED.

Mode of Inheritance

Arginase deficiency is inherited in an autosomal recessive manner.

Risk to Family Members

Parents of a proband

  • The parents of an affected child are obligate heterozygotes and therefore carry one ARG1 pathogenic variant.
  • Heterozygotes (carriers) are asymptomatic.

Sibs of a proband

  • At conception, each sib of an affected individual has a 25% chance of being affected, a 50% chance of being an asymptomatic carrier, and a 25% chance of being unaffected and not a carrier.
  • Once an at-risk sib is known to be unaffected, the risk of his/her being a carrier of an ARG1 pathogenic variant is 2/3.
  • Heterozygotes (carriers) are asymptomatic.

Offspring of a proband

  • Although most severely affected individuals have not reproduced, those who are successfully treated are likely to be fertile.
  • The offspring of an individual with arginase deficiency are obligate heterozygotes (carriers) for a pathogenic variant in ARG1.
  • The rarity of the condition makes it unlikely that an unrelated reproductive partner of the proband whose ancestors do not come from a confined geographic area will be a carrier.

Other family members of a proband. Each sib of the proband's parents is at a 50% risk of being a carrier of an ARG1 pathogenic variant.

Carrier Detection

Molecular genetic testing. Carrier testing for at-risk relatives requires prior identification of the ARG1 pathogenic variants in the family.

Biochemical genetic testing. The normal mean red blood cell arginase enzyme activity is 100 times the lower limit of detection. Thus, most obligate carriers have been easily distinguished from normal. However, in at least one instance, a mother who was an obligate carrier tested in the mid-normal range.

Related Genetic Counseling Issues

See Management, Evaluation of Relatives at Risk for information on evaluating at-risk relatives for the purpose of early diagnosis and treatment.

Family planning

  • The optimal time for determination of genetic risk, clarification of carrier status, and discussion of the availability of prenatal testing is before pregnancy.
  • It is appropriate to offer genetic counseling (including discussion of potential risks to offspring and reproductive options) to young adults who are under treatment for arginase deficiency, are carriers, or are at risk of being carriers.

DNA banking is the storage of DNA (typically extracted from white blood cells) for possible future use. Because it is likely that testing methodology and our understanding of genes, allelic variants, and diseases will improve in the future, consideration should be given to banking DNA of affected individuals.

Prenatal Testing and Preimplantation Genetic Diagnosis

Molecular genetic testing. If both ARG1 pathogenic variants have been identified in an affected family member, prenatal testing for a pregnancy at increased risk and preimplantation genetic diagnosis are possible.

Biochemical genetic testing. If molecular genetic testing is not possible, prenatal diagnosis for pregnancies at 25% risk may be possible by measuring arginase enzyme activity in fetal red blood cells obtained by percutaneous umbilical blood sampling after 18 weeks' gestation [Hewson et al 2003, Korman et al 2004].

Neither amniocytes nor chorionic villous cells normally have arginase enzyme activity and thus are unsuitable for prenatal diagnosis using biochemical testing.

Note: Gestational age is expressed as menstrual weeks calculated either from the first day of the last normal menstrual period or by ultrasound measurements.

Differences in perspective may exist among medical professionals and within families regarding the use of prenatal testing, particularly if the testing is being considered for the purpose of pregnancy termination rather than early diagnosis. While most centers would consider decisions regarding prenatal testing to be the choice of the parents, discussion of these issues is appropriate.


GeneReviews staff has selected the following disease-specific and/or umbrella support organizations and/or registries for the benefit of individuals with this disorder and their families. GeneReviews is not responsible for the information provided by other organizations. For information on selection criteria, click here.

  • National Library of Medicine Genetics Home Reference
  • National Urea Cycle Disorders Foundation
    75 South Grand Avenue
    Pasadena CA 91105
    Phone: 800-386-8233 (toll-free); 626-578-0833
    Fax: 626-578-0823
  • Metabolic Support UK
    5 Hilliards Court, Sandpiper Way
    Chester Business Park
    Chester CH4 9QP
    United Kingdom
    Phone: 0845 241 2173
  • Save Babies Through Screening Foundation, Inc.
    P. O. Box 42197
    Cincinnati OH 45242
    Phone: 888-454-3383
  • European Registry and Network for Intoxication Type Metabolic Diseases (E-IMD)
  • Urea Cycle Disorder International Patient Registry
    Phone: 626-578-0833
    Fax: 626-578-0823
  • Urea Cycle Disorders Consortium Registry
    Children's National Medical Center
    Phone: 202-306-6489

Molecular Genetics

Information in the Molecular Genetics and OMIM tables may differ from that elsewhere in the GeneReview: tables may contain more recent information. —ED.

Table A.

Arginase Deficiency: Genes and Databases

GeneChromosome LocusProteinLocus-Specific DatabasesHGMDClinVar
ARG16q23​.2Arginase-1ARG1 @ LOVDARG1ARG1

Data are compiled from the following standard references: gene from HGNC; chromosome locus from OMIM; protein from UniProt. For a description of databases (Locus Specific, HGMD, ClinVar) to which links are provided, click here.

Table B.

OMIM Entries for Arginase Deficiency (View All in OMIM)

608313ARGINASE 1; ARG1

Gene structure. ARG1 is approximately 10-15 kb in length and comprises eight exons and seven introns (see Ensembl Gene Report). For a detailed summary of gene and protein information, see Table A, Gene.

Pathogenic variants. Pathogenic variants are located throughout the coding region of the gene. Missense variants are generally found in amino acids that have been highly conserved during evolution and especially in sequences involved in the active site of the enzyme. Chain-terminating variants and deletions and insertions may be found anywhere in the gene [Vockley et al 1996]. A deletion of nearly the entire gene has also been described [Korman et al 2004].

Normal gene product. Arginase-1 is 322 amino acids long and is manganese dependent; it exists in nature as a trimer, and, unlike arginase-2, which is located in mitochondrial matrix, is located in the cytosol. The enzyme is highly stable and can be completely reactivated, if not denatured, by treating with manganese at 65° C. Expression is highest in the liver and RBCs (Reference sequence NP_000036.2).

Abnormal gene product. The mutated arginase-1 protein is rarely stable enough to be detected in the mature red blood cells of affected individuals by immunologic means.

A second, ancestral arginase gene (ARG2) located on 14q, is expressed in different tissue and cell types and may partially compensate for deficiency of arginase-1. It is thought that from an evolutionary perspective, ARG2 existed first and that ARG1 arose from it following a gene duplication event. The two gene products are more than 50% homologous at the amino acid level [Morris et al 1997, Iyer et al 1998].


Literature Cited

  • De Deyn PP, Marescau B, Qureshi IE, Cederbaum SD, Lambert M, Cerone R, Chamoles N, Specola N, Leonard JV, Gatti R, Kang SS, Mizutani N, Rezvani I, Snyderman SE, Terheggen HG, Yoshino M, Appel B, Martin JJ, Beaudet AL, Vilarinho L, Hirsch E, Jakobs K, van der Knaap MS, Naito H, Pickut BA, Shapira SK, Fuchshuber A, Roth B, Hylan K. Hyperargininemia: a treatable inborn error of metabolism? In: De Deyn PP, Marescau B, Qureshi IA, Mori A, eds. Guanidino Compounds in Biology and Medicine II. London, UK: John Libbey; 1997:53-69.
  • Hewson S, Clarke JT, Cederbaum S. Prenatal diagnosis for arginase deficiency: a case study. J Inherit Metab Dis. 2003;26:607–10. [PubMed: 14605507]
  • Iyer R, Jenkinson CP, Vockley JG, Kern RM, Grody WW, Cederbaum S. The human arginases and arginase deficiency. J Inherit Metab Dis. 1998;21 Suppl 1:86–100. [PubMed: 9686347]
  • Korman SH, Gutman A, Stemmer E, Kay BS, Ben-Neriah Z, Zeigler M. Prenatal diagnosis for arginase deficiency by second-trimester fetal erythrocyte arginase assay and first-trimester ARG1 mutation analysis. Prenat Diagn. 2004;24:857–60. [PubMed: 15565656]
  • Morris SM Jr, Bhamidipati D, Kepka-Lenhart D. Human type II arginase: sequence analysis and tissue-specific expression. Gene. 1997;193:157–61. [PubMed: 9256072]
  • Prasad AN, Breen JC, Ampola MG, Rosman NP. Argininemia: a treatable genetic cause of progressive spastic diplegia simulating cerebral palsy: case reports and literature review. J Child Neurol. 1997;12:301–9. [PubMed: 9378897]
  • Scaglia F, Lee B. Clinical, biochemical, and molecular spectrum of hyperargininemia due to arginase I deficiency. Am J Med Genet C Semin Med Genet. 2006;142C:113–20. [PMC free article: PMC4052756] [PubMed: 16602094]
  • Vockley JG, Goodman BK, Tabor DE, Kern RM, Jenkinson CP, Grody WW, Cederbaum SD. Loss of function mutations in conserved regions of the human arginase I gene. Biochem Mol Med. 1996;59:44–51. [PubMed: 8902193]

Suggested Reading

  • Boles RG, Stone ML. A patient with arginase deficiency and episodic hyperammonemia successfully treated with menses cessation. Mol Genet Metab. 2006;89:390–1. [PubMed: 16963300]
  • Crombez EA, Cederbaum SD. Hyperargininemia due to liver arginase deficiency. Mol Genet Metab. 2005;84:243–51. [PubMed: 15694174]

Chapter Notes

Author Notes

Stephen Cederbaum is Professor Emeritus of Psychiatry, Pediatrics, and Human Genetics at UCLA. His area of special interest is biochemical genetics.

Eric Crombez is a specialist in biochemical genetics. He was formerly co-director, with Dr Cederbaum, of the Urea Cycle Disorders Consortium site at UCLA and is now at Shire HGT in Cambridge, MA.

Derek Wong is Associate Clinical Professor of Pediatrics at UCLA. He is the Director of the Urea Cycle Disorders Consortium site at UCLA, and is the Head of Biochemical Genetics.

Revision History

  • 28 August 2014 (me) Comprehensive update posted live
  • 9 February 2012(me) Comprehensive update posted live
  • 5 October 2010 (cd) Revision: deletion/duplication analysis available clinically
  • 1 September 2009 (me) Comprehensive update posted live
  • 30 June 2008 (cd) Revision: sequence analysis and prenatal testing available for ARG1 mutations
  • 13 February 2007 (me) Comprehensive update posted live
  • 21 October 2004 (me) Review posted live
  • 2 March 2004 (sc) Original submission
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