Snake Venom Protein C Activators

2018 ◽  
pp. 265-279
Author(s):  
Jürg Meier ◽  
Kurt F. Stocker
Keyword(s):  
Snake Venom ◽  
Protein C ◽  
Venom Protein

Snake venom components and their cross-reactivity: a review

1989 ◽  
Vol 67 (9) ◽  
pp. 597-601 ◽  
Author(s):  
Bradley J. Berger ◽  
A. Rashid Bhatti
Keyword(s):  
Biological Activity ◽  
Snake Venom ◽  
Inorganic Compounds ◽  
Cross Reactivity ◽  
Complex Mixtures ◽  
Snake Venoms ◽  
Venom Protein

Snake venoms are complex mixtures of organic and inorganic compounds, many of which display biological activity. It has been demonstrated that antisera raised against whole venom or a single purified venom protein from one species of snake will react with proteins in the venom of other species. This cross-reactivity between species may have applications in determining snake phylogeny, but recent studies on the variation of venom components within a species make these evolutionary conclusions questionable.Key words: snake, venom, cross-reactive, evolution.

Determination of protein C in rats using the snake venom activator

1990 ◽  
Vol 4 ◽  
pp. 25
Author(s):  
S.M. Strukova ◽  
A.E. Kogan ◽  
A.A. Tara ◽  
A.A. Aaviksaar ◽  
T.N. Dugina
Keyword(s):  
Snake Venom ◽  
Protein C

Trimucytin, a collagen-like snake venom protein, activates platelets independent of I-domain within α2 subunit of α2β1 integrin

2002 ◽  
Vol 105 (2) ◽  
pp. 153-160 ◽  
Author(s):  
Chao-Zong Liu ◽  
Ting-Feng Wu ◽  
Tur-Fu Huang ◽  
Dung-Ho Wu ◽  
Guan-Ling Lin
Keyword(s):  
Snake Venom ◽  
Venom Protein ◽  
Α2β1 Integrin

Protein C functional assay using snake venom activator

1987 ◽  
Vol 47 (1) ◽  
pp. 85-91 ◽  
Author(s):  
IV Nathan ◽  
Hao Ping ◽  
MM Pradhan
Keyword(s):  
Snake Venom ◽  
Protein C ◽  
Functional Assay

The Effect of Enzymatic Removal of Sialic Acids on the Functional Properties of Protein C

1988 ◽  
Vol 60 (02) ◽  
pp. 267-270 ◽  
Author(s):  
Lena Hau ◽  
Hatem H Salem
Keyword(s):  
Sialic Acid ◽  
Functional Properties ◽  
Snake Venom ◽  
Protein C ◽  
Activated Protein C ◽  
Sialic Acids ◽  
Human Protein ◽  
Native Protein ◽  
Chromogenic Substrates ◽  
Acid Component

SummaryThe effect of enzymatic removal of sialic acid residues on the functional properties of human protein C was examined. The rates of activation of native and asialo protein C were identical using either the thrombin thrombomodulin complex or the snake venom activator, protac. Desialylated activated protein C (APC) was, two-three-fold more active than native protein C, both as an anticoagulant and in its ability to hydrolyze chromogenic substrates. The potentiating effect of the desialylation was confirmed by initially fully activating protein C followed by the desialylation process. In these studies, a two-three-fold enhancement in the activity of the protein was observed which paralleled the extent of the desialylation. The activity of asialo-protein C was completely abolished by monoclonal and polyclonal antiprotein C antibodies, confirming that the effect was mediated by APC. Our studies suggest that the sialic acid component of protein C is not essential for the expression of APC activity but may act to modulate the function of the protein.

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