Production of "internal surface reversed-phase" supports: the hydrolysis of selected substrates from silica using chymotrypsin.
The degree of hydrolysis of substrates attached to silica supports with alpha-chymotrypsin has been evaluated relative to the production of "internal surface reversed-phase" supports. The peptide substrates N-tert.-butoxycarbonyl-L-phenylalanine (Boc-L-Phe), N-carbobenzoxy-L-valine-L-phenylalanine, N-acetyl-L-phenylalanine (acetyl-L-Phe) and N-benzoyl-L-phenylalanine as well as phenylpropionic acid were attached to glycerylpropyl-bonded silica via a diamine spacer using 1,1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a coupling catalyst. The products released from the silica support on enzyme treatment were quantified by high-performance liquid chromatography. Boc-L-Phe and acetyl-L-Phe were successfully cleaved from the rigid silica matrix in high yields, whereas the remaining substrates were hydrolyzed to a lesser extent.
D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin; D006868:Hydrolysis; D007202:Indicators and Reagents; D007700:Kinetics; D012822:Silicon Dioxide
D007202:Indicators and Reagents; D012822:Silicon Dioxide; D002918:Chymotrypsin