Biochemical characterization and molecular cloning of a plasminogen activator proteinase (LV-PA) from bushmaster snake venom

2006 ◽  
Vol 1760 (12) ◽  
pp. 1762-1771 ◽  
Author(s):  
Eladio F. Sanchez ◽  
Liza F. Felicori ◽  
Carlos Chavez-Olortegui ◽  
Henrique B.P. Magalhaes ◽  
Ana L. Hermogenes ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Plasminogen Activator ◽  
Snake Venom ◽  
Biochemical Characterization

scholarly journals Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin-like snake venom enzyme.

1987 ◽  
Vol 262 (7) ◽  
pp. 3132-3135 ◽  
Author(s):  
N. Itoh ◽  
N. Tanaka ◽  
S. Mihashi ◽  
I. Yamashina
Keyword(s):  
Sequence Analysis ◽  
Molecular Cloning ◽  
Snake Venom

scholarly journals Snake Venom Hemotoxic Enzymes: Biochemical Comparison between Crotalus Species from Central Mexico

Molecules ◽  
2019 ◽  
Vol 24 (8) ◽  
pp. 1489 ◽  
Author(s):  
Octavio Roldán-Padrón ◽  
José Luis Castro-Guillén ◽  
José Alejandro García-Arredondo ◽  
Martha Sandra Cruz-Pérez ◽  
Luis Fernando Díaz-Peña ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Snake Venom ◽  
Serine Proteases ◽  
Biochemical Characterization ◽  
Protein Pattern ◽  
Medical Problem ◽  
Enzymatic Activities ◽  
Clinical Effects ◽  
Pla2 Activity ◽  
Biochemical Comparison

Snakebite envenoming is a serious medical problem in different areas of the world. In Latin America, the major prevalence is due to snakes of the family Viperidae, where rattlesnakes (Crotalus) are included. They produce hemotoxic venom which causes bleeding, tissue degradation and necrosis. Each venom has several enzymatic activities, producing different effects in the envenoming, doing its clinical effects difficult to study. Comparison between venom molecules is also difficult when different techniques are used, and therefore, their identification/characterization using the same methodology is necessary. In this work, a general biochemical characterization in snake venom of serine proteases (SVSP), phospholipases A2 (PLA2), metalloproteases (SVMP) and hyaluronidases (SVH) of Crotalus aquilus (Ca), Crotalus polystictus (Cp) and Crotalus molossus nigrescens (Cmn) was done. Differences in protein pattern, enzyme content and enzymatic activities were observed. All the venoms showed high PLA2 activity, high molecular weight SVSP, and a wide variety of SVMP and SVH forms. Ca and Cp showed the highest enzymatic activities of SVMP and SVSP trypsin-like and chymotrypsin-like, whereas Cmn showed the highest SVH and similar PLA2 activity with Ca. All the venoms showed peptides with similar molecular weight to crotamine-like myotoxins. No previous biochemical characterization of C. aquilus has been reported and there are no previous analyses that include these four protein families in these Crotalus venoms.

A new hemorrhagic metalloprotease from Bothrops jararacussu snake venom: isolation and biochemical characterization

Toxicon ◽  
2004 ◽  
Vol 44 (2) ◽  
pp. 215-223 ◽  
Author(s):  
Maurı́cio V Mazzi ◽  
Silvana Marcussi ◽  
Guilherme B Carlos ◽  
Rodrigo G Stábeli ◽  
João J Franco ◽  
...  
Keyword(s):  
Snake Venom ◽  
Biochemical Characterization ◽  
Bothrops Jararacussu

Molecular cloning and biochemical characterization of a Tau class glutathione S-transferase from Pinus brutia Ten

Trees ◽  
2020 ◽  
Vol 34 (3) ◽  
pp. 835-843
Author(s):  
Meltem Alper ◽  
Elif Öztetik ◽  
M. Yaşar Kaya ◽  
Feray Köçkar
Keyword(s):  
Molecular Cloning ◽  
Biochemical Characterization ◽  
Glutathione S Transferase ◽  
Pinus Brutia
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