Affinity chromatography on hydroxyalkyl methacrylate gels. III. Adsorption of chymotrypsin to poly(hydroxyalkyl methacrylates) with covalently bound benzyloxycarbonyl-glycyl-D-phenylalanine and -D-leucine as function of pH and ionic strength.
Chymotrypsin is specifically adsorbed at low ionic strength and alkaline pH to hydroxyalkyl methacrylate gels with N-benzyloxycarbonylglycl-D-phenylalanine or N-benzyloxycarbonylglycyl-D-leucine attached through 1,6-hexanediamine. Chymotrypsin is not adsorbed either to the unmodified gel (Spheron) or to the gel with attached, 1,6-hexanediamine (NH2-Spheron). The adsorption of chymotrypsin to Z-Gly-D-Phe-NH2-Spheron was investigated as a function of pH and ionic strength. Trypsin is not adsorbed to this gel. Chymotrypsin isolated from a crude pancreatic extract by affinity chromatography on Z-Gly-D-Phe-NH2-Spheron had the same activity as the enzyme isolated on a column of Spheron, to which the naturally-occurring trypsin inhibitor had been coupled.
D001665:Binding Sites; D002846:Chromatography, Affinity; D002918:Chymotrypsin / Q000302:isolation & purification*; D005998:Glycine; D006863:Hydrogen-Ion Concentration; D007930:Leucine; D008689:Methacrylates; D009994:Osmolar Concentration; D010649:Phenylalanine; D011485:Protein Binding
D008689:Methacrylates; D010649:Phenylalanine; D002918:Chymotrypsin; D007930:Leucine; D005998:Glycine