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Studies on receptor binding site of insulin: the hydrophobic B12Val can be substituted by hydrophilic thr
Q Q Wang1, Y M Feng, Y S Zhang
1State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry, Chinese Academy of Sciences, China.
Biochemistry and Molecular Biology International
|August 1, 1996
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.