PROTEIN-C DEGRADATION INVITRO BY NEUTROPHIL ELASTASE

被引:56
作者
ECKLE, I
SEITZ, R
EGBRING, R
KOLB, G
HAVEMANN, K
机构
来源
BIOLOGICAL CHEMISTRY HOPPE-SEYLER | 1991年 / 372卷 / 11期
关键词
PROTEIN-C; DEGRADATION; SPLIT PRODUCTS; ELASTASE;
D O I
10.1515/bchm3.1991.372.2.1007
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
Purified protein C is completely degraded into small peptides by in vitro incubation with purified elastase. Protein C is a rather sensitive substrate as degradation is already accomplished by low elastase concentrations (molar enzyme-to-substrate ratio 1:510) and short incubation periods (5 min-60 min). Protein C in a PPSB coagulation factor concentrate is equally degraded and similar split products are detected by blotting techniques. The protein C activity (measured by a chromogenic substrate) is faster reduced by elastase than the protein C concentration (measured by an ELISA). Incubation of normal plasma with high elastase concentrations (5.7 nmol/ml plasma) results in reduction of the protein C band while no split products are detectable. The pathophysiologic significance of the effects of elastase on protein C remains to be elucidated.
引用
收藏
页码:1007 / 1013
页数:7
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