Stephenson S L, Kenny A J
Biochem J. 1987 Apr 1;243(1):183-7. doi: 10.1042/bj2430183.
alpha-Human atrial natriuretic peptide, a 28-amino-acid-residue peptide, was rapidly hydrolysed by pig kidney microvillar membranes in vitro, with a t1/2 of 8 min, comparable with the rate observed with angiotensins II and III. The products of hydrolysis were analysed by h.p.l.c., the pattern obtained with membranes being similar to that with purified endopeptidase-24.11 (EC 3.4.24.11). No hydrolysis by peptidyl dipeptidase A (angiotensin I converting enzyme, EC 3.4.15.1) was observed. The contribution of the various microvillar membrane peptidases was assessed by including specific inhibitors. Phosphoramidon, an inhibitor of endopeptidase-24.11, caused 80-100% suppression of the products. Captopril and amastatin (inhibitors of peptidyl dipeptidase A and aminopeptidases respectively) had no significant effect. Hydrolysis at an undefined site within the disulphide-linked ring occurred rapidly, followed by hydrolysis at other sites, including the Ser25--Phe26 bond.
α-人心房利钠肽是一种由28个氨基酸残基组成的肽,在体外可被猪肾微绒毛膜迅速水解,半衰期为8分钟,这与血管紧张素II和III的水解速率相当。水解产物通过高效液相色谱进行分析,用膜得到的图谱与用纯化的内肽酶-24.11(EC 3.4.24.11)得到的图谱相似。未观察到肽基二肽酶A(血管紧张素I转换酶,EC 3.4.15.1)的水解作用。通过加入特异性抑制剂来评估各种微绒毛膜肽酶的作用。磷酰胺素是内肽酶-24.11的抑制剂,可导致80-100%的产物抑制。卡托普利和抑氨肽酶素(分别为肽基二肽酶A和氨肽酶的抑制剂)没有显著作用。在二硫键连接环内的一个未确定位点的水解迅速发生,随后在其他位点水解,包括Ser25-Phe26键。