Cloning and functional identification of a novel annexin subfamily in Cysticercus cellulosae.

Abstract:

:A novel cDNA was isolated from a library of Cysticercus cellulosae by immunological screening. Sequence analysis reveals that it has typical annexin structures. However, since its N-terminus is distinct and the core domain only has 32-44% amino acid identity to the tetrads of other annexins, the cDNA encodes a member of a novel annexin subfamily, which is designed as annexin B1. The recombinant protein, GST-anxB1, has the phospholipid-binding property and anticoagulatant activity common to annexins.

journal_name

Mol Biochem Parasitol

authors

Hongli Y,Shuhan S,Ruiwen C,Yingjun G

doi

10.1016/s0166-6851(01)00383-8

subject

Has Abstract

pub_date

2002-01-01 00:00:00

pages

1-5

issue

1

eissn

0166-6851

issn

1872-9428

pii

S0166685101003838

journal_volume

119

pub_type

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