NATURAL PRODUCT RESEARCH AND DEVELOPMENT ›› 2010, Vol. 23 ›› Issue (6): 929-933.

• Article •     Next Articles

Purification and Characterization of a Novel Metalloproteinase AA-MP-I from the Venom of Agkistrodon acutus

PAN Jian-ru1, HE Huo-cong2, LIU Fang2, RAO Ping-fan1*   

  1. 1Institute of Biotechnology, Fuzhou University, Fuzhou 350002, China2Fujian Provincial Tumor Hospital, Fuzhou 350014, China
  • Received:2009-03-24 Online:2011-01-10 Published:2011-10-19

Abstract:

A novel P-I snake venom metalloproteinase AA-MP-I was purified from the venom of Agkistrodon acutus by using thiophilic adsorption chromatography, Sephadex G-75, Affi-gel blue gel, and POROS HQ 20 anion-exchange chromatography. AA-MP-I was a monomer with the molecular weight of approximate 22.9 kDa on SDS-PAGE and its isoelectric point was 5.55 analyzed by IEF. AA-MP-I hasn’t any neutral carbohydrate and its N-terminal amino acid sequence was STEFQRYMEIVIVVDHSMVK. AA-MP-I has basic proteolytic and antithrombin activities, both of which are heat-unstable. In addition, AA-MP-I was proved to have hemorrhagic activity but no acidic phospholipase A2 activity.

Key words: Agkistrodon acutus, venom, metalloproteinase, antithrombin, hemorrhage activity