IS HIGH-MOLECULAR-WEIGHT-RENIN BINDING OF RENIN TO THE PROTEASE INHIBITORS AND LIPOPROTEINS

被引:4
作者
POULSEN, K [1 ]
NIELSEN, AH [1 ]
LYKKEGAARD, S [1 ]
MALLING, C [1 ]
KROLL, J [1 ]
JENSENIUS, J [1 ]
机构
[1] FINSEN INST, DK-2100 COPENHAGEN, DENMARK
来源
CLINICAL SCIENCE AND MOLECULAR MEDICINE | 1978年 / 55卷
关键词
D O I
10.1042/cs055125s
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
1. Two high-molecular-weight forms of renin (molecular weights 800 000 and 70 000) are present in mouse plasma. 2. The 800 000 form could be activated and converted into the fully active 40 000 form, by acid or limited proteolysis. The 70 000 form was activated without change in molecular weight. 3. In addition to its enzymic activity, renin was measured by a direct radioimmunoassay, which revealed that the current acid treatment of plasma did not activate all the renin present. 4. Renin is stored as fully active 40 000 renin, with a specific enzymic reactivity of 0.4 times 10(-3) GU ng(-1), in the submaxillary gland of mice. 5. Pure 125I-labelled 40 000 submaxillary renin did not bind to plasma proteins. However, by changing the tertiary structure of renin, it was bound to some of the plasma protease inhibitors; alpha2-macroglobulin, inter-alpha-trypsin inhibitor and alpha2-antithrombin. It was also bound to alpha1- and beta1-lipoprotein, albumin and an unidentified plasma protein. No binding was seen to more than 50 other studied plasma proteins.
引用
收藏
页码:S125 / S128
页数:4
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