Tateishi K, Funakoshi A, Hashimoto C, Kitayama N, Matsuoka Y
First Department of Biochemistry, School of Medicine, Fukuoka University, Japan.
Life Sci. 1992;50(9):607-13. doi: 10.1016/0024-3205(92)90246-l.
We examined the in vitro degradation of human pancreastatin-52 (hPST-52) and a larger molecular form (approximate 15 kDa) of human PST by an enzyme extract from human kidney. The PST-degrading activity was determined from the amount of immunoreactive PST remaining after incubation of hPST-52 or the larger molecular form with the enzyme extract. Human PST-52 was degraded to smaller molecular forms within 30 min, but the larger molecule was not degraded within 90 min. Phosphoramidon, an inhibitor of endopeptidase, metal ion chelators (EDTA and 1, 10-phenanthroline) and Cu2+ prevented the degradation of hPST-52. These results indicated that the enzyme in the kidney extract degraded hPST-52 and smaller forms of the peptide, but had no effect on the 15 kDa form.
我们研究了人肾酶提取物对人胰抑制素-52(hPST-52)以及人胰抑制素的一种更大分子形式(约15 kDa)的体外降解作用。通过hPST-52或更大分子形式与酶提取物孵育后剩余的免疫反应性胰抑制素的量来测定胰抑制素降解活性。人PST-52在30分钟内降解为较小的分子形式,但更大的分子在90分钟内未被降解。内肽酶抑制剂磷酰胺、金属离子螯合剂(EDTA和1,10-菲咯啉)以及Cu2+可阻止hPST-52的降解。这些结果表明,肾提取物中的酶可降解hPST-52和较小形式的肽,但对15 kDa形式无作用。