PURIFICATION OF MITOGENIC PROTEINS FROM HURA-CREPITANS AND ROBINIA-PSEUDACCACIA

被引：9
作者：
MCPHERSON, A
HOOVER, S
机构：
[1] Dept. of Biological Chemistry The Milton S. Hershey Medical Center The Pennsylvania State Univ. Hers
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 89卷 / 02期
关键词：
D O I：
10.1016/0006-291X(79)90688-0
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The lectin-mitogens from H. crepitans and R. pseudacaccia were purified by affinity chromatography and compared to that from A. precatorius by sodium lauryl sulfate gel electrophoresis. Robinia lectin is quite similar to that from A. precatorius in that it consists of 2 distinct polypeptide chains of 32,000 and 30,000 daltons, but unlike Abrus lectin the chains are not joined by disulfide bonds. Hura lectin is composed of a single polypeptide chain which migrates identically with the H chain of the Abrus lectin. This H chain is likely to be responsible for binding to galactose residues on cell surfaces. The lectin from R. pseudaccacia was obtained in crystalline form.
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页码：713 / 720
页数：8
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