Oxidation of Alpha-1-Proteinase Inhibitor: Significance for Pathobiology

1984 ◽  
pp. 89-95 ◽  
Author(s):  
James Travis ◽  
Keith Beatty ◽  
Nancy Matheson
Keyword(s):  
Proteinase Inhibitor

Some Properties of an Antiplasmin Substance from Rabbit Platelets

1970 ◽  
Vol 24 (01/02) ◽  
pp. 076-084 ◽  
Author(s):  
K Wakabayashi ◽  
K Fujikawa ◽  
T Abe
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Rabbit Platelets

SummaryRabbit platelets contained a proteinase inhibitor which inhibited plasmin, trypsin and chymotrypsin activities, and serum kallikrein to some extent. It did not inhibit pancreatic kallikrein and thrombin. It reacted stoechiometrically with these enzymes in a prompt fashion and was found to have a molecular weight of about 40,000.

scholarly journals Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.

1992 ◽  
Vol 267 (3) ◽  
pp. 1990-1994
Author(s):  
P Chen ◽  
J Rose ◽  
R Love ◽  
C H Wei ◽  
B C Wang
Keyword(s):  
Proteinase Inhibitor ◽  
Trypsin Inhibitors

scholarly journals Heparin strongly decreases the rate of inhibition of neutrophil elastase by alpha 1-proteinase inhibitor

1991 ◽  
Vol 266 (23) ◽  
pp. 15356-15362
Author(s):  
K.J. Frommherz ◽  
B. Faller ◽  
J.G. Bieth
Keyword(s):  
Neutrophil Elastase ◽  
Proteinase Inhibitor
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