J Biochem. 1981 Dec;90(6):1787-93.

Autolysis of calcium-activated neutral protease of chicken skeletal muscle.

Suzuki K, Tsuji S, Ishiura S, Kimura Y, Kubota S, Imahori K.

Abstract

The conditions and process of autolysis of calcium-activated neutral protease (CANP) were examined. Optimal conditions for autolysis were the same as those required for expression of activity of CANP. The autolysis proceeded rapidly by a strictly limited proteolysis. During autolysis the molecular weight of CANP changed from 82 K (native CANP or mCANP) to 79 K and then 60 K. The 79 K and 60 K molecular species were both active at microM order of Ca2+ (muCANP), whereas the native CANP is active at mM order of Ca2+ (mCANP). Various proteases examined did not produce muCANP from mcanp under the conditions tested. Furthermore, muCANP did not yield muCANP from mCANP at lower Ca2+ concentrations where only muCANP was active. Therefore, muCANP is produced from mCANP only by the specific autolysis of mCANP.

PMID:: 6277879; [PubMed - indexed for MEDLINE]

Free full text

LinkOut - more resources

Full Text Sources

Molecular Biology Databases

Supplemental Content

Save items

Related citations in PubMed

Effect of metal ions on the structure and activity of calcium-activated neutral protease (CANP). [J Biochem. 1983]
Effect of metal ions on the structure and activity of calcium-activated neutral protease (CANP).
Suzuki K, Ishiura S. J Biochem. 1983 Jun; 93(6):1463-71.
Comparison of calcium-activated neutral proteases from skeletal muscle of rabbit and chicken. [J Biochem. 1984]
Comparison of calcium-activated neutral proteases from skeletal muscle of rabbit and chicken.
Kawashima S, Nomoto M, Hayashi M, Inomata M, Nakamura M, Imahori K. J Biochem. 1984 Jan; 95(1):95-101.
Comparison of low and high calcium requiring forms of the calcium-activated neutral protease (CANP) from rabbit skeletal muscle. [J Biochem. 1984]
Comparison of low and high calcium requiring forms of the calcium-activated neutral protease (CANP) from rabbit skeletal muscle.
Inomata M, Nomoto M, Hayashi M, Nakamura M, Imahori K, Kawashima S. J Biochem. 1984 Jun; 95(6):1661-70.
Review Calcium-activated neutral protease (CANP) in brain and other tissues. [Prog Neurobiol. 1984]
Review Calcium-activated neutral protease (CANP) in brain and other tissues.
Zimmerman UJ, Schlaepfer WW. Prog Neurobiol. 1984; 23(1-2):63-78.
Review Proteinases in cardiac and skeletal muscle. [Fed Proc. 1980]
Review Proteinases in cardiac and skeletal muscle.
Bird JW, Carter JH, Triemer RE, Brooks RM, Spanier AM. Fed Proc. 1980 Jan; 39(1):20-5.

See reviews... See all...

Cited by 8 PubMed Central articles

Review Calpain chronicle--an enzyme family under multidisciplinary characterization. [Proc Jpn Acad Ser B Phys Biol ...]
Review Calpain chronicle--an enzyme family under multidisciplinary characterization.
Sorimachi H, Hata S, Ono Y. Proc Jpn Acad Ser B Phys Biol Sci. 2011; 87(6):287-327.
Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. [Proc Natl Acad Sci U S A. 1993]
Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration.
Saito K, Elce JS, Hamos JE, Nixon RA. Proc Natl Acad Sci U S A. 1993 Apr 1; 90(7):2628-32.
Studies of the active site of m-calpain and the interaction with calpastatin. [Biochem J. 1993]
Studies of the active site of m-calpain and the interaction with calpastatin.
Crawford C, Brown NR, Willis AC. Biochem J. 1993 Nov 15; 296 ( Pt 1):135-42.

See all...

Related information

Related Citations
Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
Compound (MeSH Keyword)
PubChem chemical compound records that are classified under the same Medical Subject Headings (MeSH) controlled vocabulary as the current articles.
Substance (MeSH Keyword)
PubChem chemical substance (submitted) records that are classified under the same Medical Subject Headings (MeSH) controlled vocabulary as the current articles.
Cited in PMC
Full-text articles in the PubMed Central Database that cite the current articles.

Recent activity

Clear Turn Off Turn On

Autolysis of calcium-activated neutral protease of chicken skeletal muscle.
Autolysis of calcium-activated neutral protease of chicken skeletal muscle.
J Biochem. 1981 Dec ;90(6):1787-93.

PubMed
Ion transport in yeast.
Ion transport in yeast.
Biochim Biophys Acta. 1981 Dec ;650(2-3):88-127.

PubMed
Experimental osteomyelitis. V. Therapeutic trials with oxacillin and sisomicin a...
Experimental osteomyelitis. V. Therapeutic trials with oxacillin and sisomicin alone and in combination.
J Infect Dis. 1978 Feb ;137(2):155-60.

PubMed
A variant of adrenomyeloneuropathy with hypothalamic-pituitary dysfunction and n...
A variant of adrenomyeloneuropathy with hypothalamic-pituitary dysfunction and neurologic remission after glucocorticoid replacement therapy.
Am J Med. 1982 Jan ;72(1):173-6.

PubMed
Survival after early and normal retirement.
Survival after early and normal retirement.
J Gerontol. 1978 Mar ;33(2):269-78.

PubMed

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

PubMed

Result Filters

Display Settings:

Send to:

Autolysis of calcium-activated neutral protease of chicken skeletal muscle.

Abstract

Publication Types, MeSH Terms, Substances

Publication Types

MeSH Terms

Substances

LinkOut - more resources

Full Text Sources

Molecular Biology Databases

Supplemental Content

Save items

Related citations in PubMed

Cited by 8 PubMed Central articles

Related information

Recent activity

Simple NCBI Directory

Getting Started

Resources

Popular

Featured

NCBI Information