copper(ii)-iminodiacetate and benzoyltyrosine-ethyl-ester

copper(ii)-iminodiacetate has been researched along with benzoyltyrosine-ethyl-ester* in 1 studies

Other Studies

1 other study(ies) available for copper(ii)-iminodiacetate and benzoyltyrosine-ethyl-ester

Article	Year
Structure-function relationship in glycosylated alpha-chymotrypsin as probed by IMAC and IMACE. Biochimica et biophysica acta, 1999, Aug-17, Volume: 1433, Issue:1-2 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. Topics: Animals; Caseins; Cattle; Chromatography, Affinity; Chymotrypsin; Electrophoresis, Capillary; Glucosamine; Glycosylation; Histidine; Hydrogen Bonding; Imino Acids; Mass Spectrometry; Metals; Structure-Activity Relationship; Tyrosine	1999

Article

Year

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

Biochimica et biophysica acta, 1999, Aug-17, Volume: 1433, Issue:1-2

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.

Topics: Animals; Caseins; Cattle; Chromatography, Affinity; Chymotrypsin; Electrophoresis, Capillary; Glucosamine; Glycosylation; Histidine; Hydrogen Bonding; Imino Acids; Mass Spectrometry; Metals; Structure-Activity Relationship; Tyrosine

1999