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Isomeric and quaternary properties of homogenous 33 kDa protein from the venom of chelonus near curvimaculatus
Author(s) -
Jones Davy,
Krishnan Anuradha,
Sarkari Neville,
Wozniak Mietek
Publication year - 1994
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940260203
Subject(s) - biology , isoelectric focusing , biochemistry , venom , complementary dna , denaturation (fissile materials) , glycoprotein , protein quaternary structure , structural similarity , microbiology and biotechnology , protein subunit , chemistry , gene , enzyme , nuclear chemistry
The 33,000 Dalton venom protein of Chelonus near curvimaculatus was characterized for structural properties of charge, quaternary associations, and relationship to polydnavirus encoded proteins. Homogenous isoforms of the protein were isolated from the venom by sequential steps of (1) microdissection, (2) separation based on charge (Mono‐Q column HPLC or narrow‐range electrofocusing), and (3) centrifugal filtration based on molecular weight using Centricon microconcentrators. The purified protein dimerized under native conditions, and this quaternary association became denaturation resistant under certain conditions. Chemical modification of lysine epsilon amino groups did not disrupt such dimerization. The cDNA for the protein did not possess high similarity to any sequence encoded in the polydnavirus, as indicated by results of Southern blotting, but does possess similarity in its repeats to the repeats of the immunologically protective surface glycoprotein of Leishmania amazonensis . © 1994 Wiley‐Liss, Inc.