| Title : Purification and cloning of cysteine-rich proteins from Trimeresurus jerdonii and Naja atra venoms - Jin_2003_Toxicon_42_539 |
| Author(s) : Jin Y , Lu Q , Zhou X , Zhu S , Li R , Wang W , Xiong Y |
| Ref : Toxicon , 42 :539 , 2003 |
| Abstract : Three 26 kDa proteins, named as TJ-CRVP, NA-CRVP1 and NA-CRVP2, were isolated from the venoms of Trimeresurus jerdonii and Naja atra, respectively. The N-terminal sequences of TJ-CRVP and NA-CRVPs were determined. These components were devoid of the enzymatic activities tested, such as phospholipase A(2), arginine esterase, proteolysis, L-amino acid oxidase, 5'nucleotidase, acetylcholinesterase. Furthermore, these three components did not have the following biological activities: coagulant and anticoagulant activities, lethal activity, myotoxicity, hemorrhagic activity, platelet aggregation and platelet aggregation-inhibiting activities. These proteins are named as cysteine-rich venom protein (CRVP) because their sequences showed high level of similarity with mammalian cysteine-rich secretory protein (CRISP) family. Recently, some CRISP-like proteins were also isolated from several different snake venoms, including Agkistrodon blomhoffi, Trimeresurus flavoviridis, Lanticauda semifascita and king cobra. We presumed that CRVP might be a common component in snake venoms. Of particular interest, phylogenetic analysis and sequence alignment showed that NA-CRVP1 and ophanin, both from elapid snakes, share higher similarity with CRVPs from Viperidae snakes. |
| ESTHER : Jin_2003_Toxicon_42_539 |
| PubMedSearch : Jin_2003_Toxicon_42_539 |
| PubMedID: 14529736 |
Jin Y, Lu Q, Zhou X, Zhu S, Li R, Wang W, Xiong Y (2003)
Purification and cloning of cysteine-rich proteins from Trimeresurus jerdonii and Naja atra venoms
Toxicon
42 :539
Jin Y, Lu Q, Zhou X, Zhu S, Li R, Wang W, Xiong Y (2003)
Toxicon
42 :539