Isomeric and quaternary properties of homogenous 33 kDa protein from the venom of Chelonus near curvimaculatus.
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.
Jones
D
D
Graduate Center for Toxicology, University of Kentucky, Lexington 40506.
Krishnan
A
A
Sarkari
N
N
Wozniak
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D018071:Polydnaviridae; D011487:Protein Conformation; D012091:Repetitive Sequences, Nucleic Acid; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins / Q000737:chemistry; D014862:Wasp Venoms / Q000737:chemistry* / Q000302:isolation & purification; D014863:Wasps
D014764:Viral Proteins; D014862:Wasp Venoms