@article{oai:soar-ir.repo.nii.ac.jp:00010598, author = {Sato, K and Tadasa, K and Kayahara, H}, issue = {1-2}, journal = {信州大学農学部紀要}, month = {Dec}, note = {To investigate the interaction of proteases (thermolysin, α-chymotrypsin, papain and pepsin) with organic solvent molecules, buffer systems in which n-alcohols were dissolved as to make a one-phase medium were used in the case of peptide synthesis or Z-amino acid hydrolysis as model reactions. The chain length of n-alcohols gave different characteristics of the effective patterns to the enzymes, and also each protease was affected in different modes of effective profiles by n-alcohols. Activity of α-chymotrypsin was increased by n-alcohols higher than n-hexanol grdually with increase of their concentration just over the saturation to the buffer. The activation was proposed to be non-essential by kinetics. Meanwhile, n-pentanol to α-chymotrypsin showed to be an uncompetitive inhibitor., Article, 信州大学農学部紀要. 32(1-2): 15-22 (1995)}, pages = {15--22}, title = {Variety of Effect of n-Alcohols on Microenvironment of Some Proteases in Peptide Synthesis or Z (N-Benzyloxycarbonyl) : Amino Acid Ester Hydrolysis}, volume = {32}, year = {1995} }