Purification and properties of insulin receptors from rat liver membranes
阅读量：
22
摘要：
Insulin receptors were solubilized from rat liver membranes with Triton X-100. The soluble receptors were purified on DEAE cellulose and then on an insulin-agarose affinity column. The purified receptor had a Stokes radius of 72Å on Sepharose 6B, an isoelectric point of 4.0, and could be adsorbed to Conanavalin A-agarose and specifically eluted with α-methylmannopyranoside. The eluate from the insulin-agarose column demonstrated a major band with an apparent molecular weight of 135,000 on SDS polyacrylamide gel electrophoresis. Because of the possibility of anomalous SDS binding, this molecular weight must be accepted with caution.
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关键词：
adjustment of factors adjusted orthogonality factorial experiment nonorthogonal design pairwise orthogonality
DOI：
10.1016/S0006-291X(77)80074-0
被引量：
年份：
1977
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