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1.
Figure 4

Figure 4. From: Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of ?-oxidation in insulin secretion.

Diagram of aligned SCHAD sequences from several evolutionarily distant species. Pro258 (in bold), which is replaced by Leu in the DNA of FS, is completely conserved in the SCHAD coding sequences from different species, including bacteria. Human, NP_005318; Pig, AAD20939; Caenorhabditis elegans, P41938; Clostridium acetobutylicum, AAA95971.

Peter T. Clayton, et al. J Clin Invest. 2001 August 1;108(3):457-465.
2.
Figure 1

Figure 1. From: Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of ?-oxidation in insulin secretion.

Analysis of butyl esters of carnitine and acylcarnitine species in a blood spot from FS. Peak identities are: m/z 218, free carnitine; 227, D9-carnitine; 260, acetyl-carnitine; 263, D3-acetylcarnitine; 277, D3-propionylcarnitine; 304, hydroxybutyrylcarnitine; 347, D3-octanoylcarnitine; 456, palmitoylcarnitine ; 459, D3-palmitoylcarnitine; and 482, oleoylcarnitine.

Peter T. Clayton, et al. J Clin Invest. 2001 August 1;108(3):457-465.
3.
Figure 6

Figure 6. From: Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of ?-oxidation in insulin secretion.

The two postulated pathways for β cell signaling (from ref. 14). PDH, pyruvate dehydrogenase; PC, pyruvate carboxylase; CL, citrate lyase; CPT1, carnitine palmitoyl transferase 1; m, mitochondrial; c, cytosolic; AcCoa, acetyl-CoA; LCFA-CoA, long-chain fatty acyl-CoA.

Peter T. Clayton, et al. J Clin Invest. 2001 August 1;108(3):457-465.
4.
Figure 2

Figure 2. From: Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of ?-oxidation in insulin secretion.

Western blot analysis of SCHAD in fibroblasts. Fibroblast homogenates (100 μg protein) were analyzed by SDS-PAGE, electroblotted, and visualized by reaction with rabbit anti-SCHAD and ECL+. The results were compared with purified pig heart SCHAD, bovine liver SCHAD, and a rat liver mitochondrial preparation (protein loadings shown).

Peter T. Clayton, et al. J Clin Invest. 2001 August 1;108(3):457-465.
5.
Figure 5

Figure 5. From: Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of ?-oxidation in insulin secretion.

Expression of wild-type and C773T mutant SCHAD using a reticulocyte lysate system. (a) Western blot showing no protein with vector alone, immunoreactive SCHAD protein with an apparent molecular weight of 35 kDa with the wild-type SCHAD construct, and immunoreactive SCHAD protein with a slightly lower apparent molecular weight with the C773T mutant construct. (b) SCHAD enzyme activity obtained with expression of the wild-type and C773T mutant SCHAD proteins. Enzyme activity is equal to the nanomole substrate converted per microliter of reticulocyte lysate between 10 and 30 minutes’ incubation.

Peter T. Clayton, et al. J Clin Invest. 2001 August 1;108(3):457-465.
6.
Figure 3

Figure 3. From: Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of ?-oxidation in insulin secretion.

Restriction fragment length analysis of DNA fragments containing nt 773 of the SCHAD coding sequence. DNA from FS, her parents, and controls was amplified using primers for exon 7 (Table 2). The PCR product was analyzed on a 2% agarose gel, either untreated (lane 1) or after exposure to ApaI for 2 hours (lanes 2–5). The C773T mutation abrogates an ApaI restriction site present in the normal sequence. ApaI digestion of the DNA fragment from controls yields two bands of 121 and 171 nt (asterisk). Exposure of the mutated sequence to ApaI yields a single band of 292 nt (arrow). Lane 1, patient DNA fragment (untreated); lane 2, DNA fragment of the father after ApaI treatment; lane 3, DNA fragment of the mother after ApaI treatment; lane 4, DNA fragment of the patient treated with ApaI; lane 5, DNA fragment of a control treated with ApaI. The pattern of the DNA fragments of the parents reveals the presence of both the normal and the mutated sequence.

Peter T. Clayton, et al. J Clin Invest. 2001 August 1;108(3):457-465.

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