In Vitro Pepsin Digestion Characteristics of Silver Carp (Hypophthalmichthys molitrix) Surimi Gels with Different Degrees of Cross-Linking Induced by Setting Time and Microbial Transglutaminase

2020 ◽  
Vol 68 (31) ◽  
pp. 8413-8430 ◽  
Author(s):  
Mengxue Fang ◽  
Shanbai Xiong ◽  
Yue Jiang ◽  
Tao Yin ◽  
Yang Hu ◽  
...  
Keyword(s):  
Setting Time ◽  
Silver Carp ◽  
Microbial Transglutaminase ◽  
Cross Linking ◽  
Hypophthalmichthys Molitrix ◽  
Pepsin Digestion

Tridegin, a Novel Peptidic Inhibitor of Factor XIIIa from the Leech, Haementeria ghilianii, Enhances Fibrinolysis In Vitro

1997 ◽  
Vol 77 (05) ◽  
pp. 0959-0963 ◽  
Author(s):  
Lisa Seale ◽  
Sarah Finney ◽  
Roy T Sawyer ◽  
Robert B Wallis
Keyword(s):  
Potent Inhibitor ◽  
Platelet Rich Plasma ◽  
Factor Xiiia ◽  
Cross Linking ◽  
Fibrinolytic Enzymes ◽  
Small Polypeptide ◽  
Tissue Plasminogen ◽  
Protein Cross Linking

SummaryTridegin is a potent inhibitor of factor Xllla from the leech, Haementeria ghilianii, which inhibits protein cross-linking. It modifies plasmin-mediated fibrin degradation as shown by the absence of D-dimer and approximately halves the time for fibrinolysis. Plasma clots formed in the presence of Tridegin lyse more rapidly when either streptokinase, tissue plasminogen activator or hementin is added 2 h after clot formation. The effect of Tridegin is markedly increased if clots are formed from platelet-rich plasma. Platelet-rich plasma clots are lysed much more slowly by the fibrinolytic enzymes used and if Tridegin is present, the rate of lysis returns almost to that of platelet- free clots. These studies indicate the important role of platelets in conferring resistance to commonly used fibrinolytic enzymes and suggest that protein cross-linking is an important step in this effect. Moreover they indicate that Tridegin, a small polypeptide, may have potential as an adjunct to thrombolytic therapy.

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