Purification of mitogenic proteins from hura crepitans and Robinia pseudaccacia
Volume: 89, Issue: 2, Pages: 713 - 720
Published: Jul 1, 1979
Abstract
The lectin-mitogens from Hura crepitans and Robinia pseudacaccia have been purified by affinity chromatography and compared to that from Abrus precatorius by sodium lauryl sulfate gel electrophoresis. Robinia lectin is quite similar to that from Abrus precatorius in that it consists of two distinct polypeptide chains of 32,000 and 30,000 daltons but unlike abrus lectin the chains are not joined by disulphide bonds. Hura lectin is composed of...
Paper Details
Title
Purification of mitogenic proteins from hura crepitans and Robinia pseudaccacia
Published Date
Jul 1, 1979
Volume
89
Issue
2
Pages
713 - 720
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