A spider toxin binding protein from bovine brain: its purification and N-terminal amino acid sequence determination.
A 60kDa spider toxin binding protein from bovine brain was solubilized with digitonin and purified up to 5800-folds over starting crude homogenate. The purification procedure entailed DEAE-cellulose, concanavalin-A affinity, 1-naphthylacetyl spermine affinity and high performance liquid chromatography. The purified protein owned a very high affinity for ligand 125I-JSTX-3 binding Kd 15.6nM and Bmax 6.5nM. The amino acid composition of the protein was determined. The N-terminal amino acid sequence analysis yielded a unique sequence: NH2-X-Pro-X-Val-Tyr-Phe-Lys-Glu-Gln-Phe-Leu-Asp-Gly-Asp-X.
Hossain
A
A
Department of Analytical Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Hagiwara
K
K
Kawai
N
N
Nakajima
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry; D002352:Carrier Proteins / Q000032:analysis / Q000302:isolation & purification*; D002417:Cattle; D008969:Molecular Sequence Data
D002352:Carrier Proteins; C073512:JSTX-3 binding protein, bos taurus