ON SOME AUTOLYZED DERIVATIVES OF BOVINE TRYPSIN

被引:63
作者
MAROUX, S
DESNUELLE, P
机构
[1] Centre de Biochimie et de Biologie Moléculaire, C.N.R.S., Marseille
关键词
D O I
10.1016/0005-2795(69)90227-X
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
Chromatography or incubation of dilute solutions of bovine trypsin at 4° and pH 5.5 in the presence of Ca2+ appears to induce almost exclusively the autolytic cleavage of bond Arg105-Val106. Bonds Lys49-Ser50 and Lys131-Ser132 are also found substantially autolyzed in commercial trypsin preparations. Evidence is presented suggesting that trypsin still retain activity after cleavage of bonds Arg105-Val106 and Lys131-Ser132. In contrast, the cleavage of bond Lys49-Ser50, close to residue His46, probably inactivates the enzyme. © 1969.
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页码:59 / +
页数:1
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