A SPIDER TOXIN BINDING-PROTEIN FROM BOVINE BRAIN - ITS PURIFICATION AND N-TERMINAL AMINO-ACID-SEQUENCE DETERMINATION

被引：0
|
作者：
HOSSAIN, A [1 ]
HAGIWARA, K [1 ]
KAWAI, N [1 ]
NAKAJIMA, T [1 ]
机构：
[1] JICHI IKA UNIV, DEPT PHYSIOL 1, TOCHIGI 32904, JAPAN
来源：
CHEMICAL & PHARMACEUTICAL BULLETIN | 1991年 / 39卷 / 11期
关键词：
SPIDER TOXIN BINDING PROTEIN; GLUTAMATE RECEPTOR; 1-NAPHTHYLACETYL SPERMINE AFFINITY CHROMATOGRAPHY; N-TERMINAL AMINO ACID ANALYSIS; !text type='JS']JS[!/text]TX-3; EXCITATORY POSTSYNAPTIC POTENTIAL;
D O I：
暂无
中图分类号：
R914 [药物化学];
学科分类号：
100701 ;
摘要：
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 I-125-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-.
引用
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页码：3079 / 3081
页数：3
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