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Zoological Research
Kunming Institute of Zoology, Chinese Academy of Sciences
ISSN: 2095-8137
Vol. 26, No. 4, 2005, pp. 404-409
Bioline Code: zr05029
Full paper language: Chinese
Document type: Research Article
Document available free of charge

Zoological Research, Vol. 26, No. 4, 2005, pp. 404-409

 en Purification and Characterization of Annexin Ⅱ Related Protein from Bombina maxina check for this species in other resources Skin
ZHANG Jie, WEI Shuang-shuang, ZHANG Yong, ZHANG Ying-xia, LEE Wen-hui

Abstract

A single chain protein with an apparent molecular weight of 33 kDa was purified from skin of Bombina maxima check for this species in other resources by a combination of ion exchange and gel filtration chromatography steps. N-terminal amino acid sequence determination indicated that it shares 70%, 64% and 56% identity with those of annexin II from the African claw toad, red jungle fowl and human, respectively. The purified protein from B. maxina inhibits stejnulxin (a specific platelet agonist via platelet membrane glycoprotein VI receptor) induced platelet aggregation in a Ca2+ dependent manner. Maximal inhibition rate reaches 48%. Based on the N-terminal amino acid sequence BLAST search results and the fact that its activity is strictly Ca2+ dependent, the purified protein might be structurally and functionally related to the annexin protein family.

Keywords
Amphibian, Annexin II, Bombina maxina, Platelet, Stejulnxin

 
© Copyright 2005 Kunming Institute of Zoology, the Chinese Academy of Sciences
Alternative site location: http://www.zoores.ac.cn/

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