Heparin and its Derivatives Modulate Serine Proteinases (SERPS) Serine Proteinase Inhibitors (SERPINS) Balance

1994 ◽  
Vol 190 (9-10) ◽  
pp. 895-902 ◽  
Author(s):  
W. Hornebeck ◽  
C. Lafuma ◽  
L. Robert ◽  
M. Móczár ◽  
E. Móczár
Biochimie ◽  
2004 ◽  
Vol 86 (9-10) ◽  
pp. 643-649 ◽  
Author(s):  
Sergio Daishi Sasaki ◽  
Simone Sant’Anna Azzolini ◽  
Izaura Yoshico Hirata ◽  
Renato Andreotti ◽  
Aparecida Sadae Tanaka

1984 ◽  
Vol 218 (3) ◽  
pp. 953-959 ◽  
Author(s):  
L Kuehn ◽  
M Rutschmann ◽  
B Dahlmann ◽  
H Reinauer

Three different serine proteinase inhibitors were isolated from rat serum and purified to apparent homogeneity. One of the inhibitors appears to be homologous to alpha 1-proteinase inhibitor isolated from man and other species, but the other two, designated rat proteinase inhibitor I and rat proteinase inhibitor II, seem to have no human counterpart. alpha 1-Proteinase inhibitor (Mr 55000) inhibits trypsin, chymotrypsin and elastase, the three serine proteinases tested. Rat proteinase inhibitor I (Mr 66000) is active towards trypsin and chymotrypsin, but is inactive towards elastase. Rat proteinase inhibitor II (Mr 65000) is an effective inhibitor of trypsin only. Their contributions to the trypsin-inhibitory capacity of rat serum are about 68, 14 and 18% for alpha 1-proteinase inhibitor, rat proteinase inhibitor I and rat proteinase inhibitor II respectively.


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