DUAL NATURE OF THE REACTION BETWEEN PORCINE ELASTASE AND HUMAN-PLASMA ALPHA-1-PROTEINASE INHIBITOR

被引:52
作者
SATOH, S
KURECKI, T
KRESS, LF
LASKOWSKI, M
机构
[1] Laboratory of Enzymology, Roswell Park Memorial Institute Buffalo
关键词
D O I
10.1016/0006-291X(79)90391-7
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
Only a portion of human plasma α1 proteinase inhibitor (α1PI) forms a 1:1 complex with porcine elastase; the other portion is inactivated via proteolysis. High temperature (37°) and high salt (2 M) enhance complex formation. The complex is unstable, but no significant liberation of active elastase could be demonstrated. Probably the same two major products of ∼50,000 and ∼4,000 daltons are formed from α1PI via proteolysis and via disintegration of the complex. Iodination of α1PI or oxidation with chloramine-T prevents complex formation with elastase but not with trypsin. Iodinated elastase, however, forms a complex with α1PI. © 1979.
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页码:130 / 137
页数:8
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