INSULIN VOM SCHLEIMFISCH (MYXINE GLUTINOSA CYCLOSTOMATA)

被引:17
作者
WEITZEL, G
STRATLING, WH
HAHN, J
MARTINI, O
机构
来源
HOPPE-SEYLERS ZEITSCHRIFT FUR PHYSIOLOGISCHE CHEMIE | 1967年 / 348卷 / 05期
关键词
D O I
10.1515/bchm2.1967.348.1.525
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
The insulin of the hag fish Myxine glutinosa was isolated, cleaved by oxidation and separated into A and B chains. The N-terminal amino acids are glycine (A-chain) and phenyla-lanine (B-chain); the C-terminal amino acids are asparagine (A-chain) and probably a basic amino acid (B -chain). The A-chain contains no phenylalanine. One histidine of the B-chain is replaced by a different amino acid. The intact insulin and its separate chains, especially the A-chain, are more basic than any other hitherto known insulin or its chains. In the immunological test with the double antibody method, the activity is about 0.1%. In the fatpad assay with the rat, the hag fish insulin has an activity of about 7% (bovine insulin = 100%), equivalent to about 2 lU/mg. The yield is about 3 mg insulin/g. fresh endocrinal pancreas.
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页码:525 / +
页数:1
相关论文
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