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  • Structure-function relationship in glycosylated alpha-chymotrypsin as probed by IMAC and IMACE.

Structure-function relationship in glycosylated alpha-chymotrypsin as probed by IMAC and IMACE.

Biochimica et biophysica acta (1999-08-14)
K Y Jiang, O Pitiot, M Anissimova, H Adenier, M A Vijayalakshmi
摘要

Chemical glycosylation of bovine alpha-chymotrypsin, by a glucosamine adduct on the carboxyl group, results in the modification of its catalytic activity. The structural alterations of alpha-chymotrypsin resulting from its glycosylation are studied by immobilized metal-ion affinity chromatography (IMAC) and immobilized metal-ion affinity capillary electrophoresis (IMACE). The chemical glycosylation of alpha-chymotrypsin generates two distinct subpopulations of the protein: one which totally loses the initial affinity for IDA-Cu(II) and another which exhibits an increased affinity for the metal chelate ligand.

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Sigma-Aldrich
α-糜蛋白酶 来源于牛胰腺, Type II, lyophilized powder, ≥40 units/mg protein
Sigma-Aldrich
N-苯甲酰基-L-酪氨酸乙酯
Sigma-Aldrich
N-苯甲酰基-L-酪氨酸乙酯, ≥98.0% (NT)