Studies of the enzymatic degradation of β-casomorphins
Studies of the enzymatic degradation of β-casomorphins
复制标题
β-酪啡肽酶降解的研究
DOI：
10.1016/0024-3205(83)90463-0
复制
发表时间：
1983
期刊：
影响因子：
6.1
通讯作者：
H. Teschemacher
中科院分区：
文献类型：
--
作者：
G. Kreil;M. Umbach;V. Brantl;H. Teschemacher
β-酪啡肽(β-CMS)虽然对蛋白水解酶具有高度的抗性，但在牛或大鼠血浆中被证明是快速降解的。这些由氨基酸序列TYR-PRO-Phe-GLY-PRO-Ile及其C端缩短片段组成的多肽的降解可能是由于一种与二肽基多肽酶IV(DP IV)相同或相似的酶所致，该酶可将二肽片段从多肽的N端切割下来，位于Pro残基之后。这一假设与β-酪吗啡素(β-CM)类似物的发现是一致的，其中第2位的Pro残基被D-丙氨酸取代，似乎完全抵抗血浆中的酶攻击。
β-Casomorphins (β-CMs), although known to be highly resistant to proteolytic enzymes, are demonstrated to be rapidly degraded in bovine or rat plasma. Degradation of these peptides consisting of the amino acid sequence TYR-PRO-PHE-GLY-PRO-ILE and C-terminally shortened fragments thereof, may be due to an enzyme identical with or similar to the dipeptidyl-peptidase IV (DP IV) which is known to cleave dipeptide fragments from the N-terminus of peptides after proline residues. This assumption is compatible with the finding that β-casomorphin (β-CM) analogues in which the proline residue in position two has been replaced by D-alanine, seem to be completely resistant to enzymatic attack in the plasma.