Studies on receptor binding site of insulin: the hydrophobic B12Val can be substituted by hydrophilic thr.
作者信息
Wang Q Q, Feng Y M, Zhang Y S
机构信息
State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry, Chinese Academy of Sciences, China.
出版信息
Biochem Mol Biol Int. 1996 Aug;39(6):1245-54. doi: 10.1080/15216549600201442.
PMID:8876979
Abstract
[B12Thr]human insulin and [B12Leu]human insulin were obtained by means of site-directed random mutagenesis. [B12Thr]human insulin retain total biological activity but [B12Leu]human insulin has much lower biological activity. Receptor binding activities of [B12Thr]human insulin and [B12Leu]human insulin are 56% and 3%, respectively, as that of native porcine insulin. The results suggest that the hydrophobic property of the residue side chain at B12 may not be necessary.
摘要
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