PURIFICATION AND AMINO-TERMINAL SEQUENCE OF RAT-KIDNEY RENIN - EVIDENCE FOR A 2-CHAIN STRUCTURE

被引:10
作者
CAMPBELL, DJ [1 ]
VALENTIJN, AJ [1 ]
CONDRON, R [1 ]
机构
[1] LA TROBE UNIV,DEPT BIOCHEM,BUNDOORA,VIC 3083,AUSTRALIA
关键词
RENIN; PRORENIN; PURIFICATION; AMINO ACID SEQUENCE; RAT KIDNEY;
D O I
10.1097/00004872-199101000-00005
中图分类号
R6 [外科学];
学科分类号
1002 ; 100210 ;
摘要
Rat kidney renin was purified 29 000-fold using a nine-step procedure with a 4% recovery. N-terminal sequence analysis of the non-reduced renin revealed two sequences, indicating a two-chain structure. When compared with the amino acid sequence deduced from the rat preprorenin cDNA sequence, the N-termini of the A and B chains were residues 72 and 355, respectively, of preprorenin. The two-chain structure was confirmed by sodium dodecyl sulphate polyacrylamide gel electrophoresis. Rat kidney renin migrated as two broad bands of 35 000-36 000 and 37 000-38 000 Da under non-reducing conditions. Under reducing conditions, the size of both bands decreased by approximately 3000 Da and a band migrated at the buffer front (approximately 5000 Da). The site of cleavage between the two chains of rat renin is analogous to that of mouse submandibular gland renin. However, processing of the prosequence of rat prorenin differs from that of mouse and human prorenin, indicating that the mechanism of activation of prorenin is species-specific.
引用
收藏
页码:29 / 33
页数:5
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