ADDITIONAL DATA ABOUT THERMOLYSIN SPECIFICITY IN BUFFER-CONTAINING AND GLYCEROL-CONTAINING MEDIA

Synthesis and use of various substrates permit an improved approach to thermolysin-peptide recognition and elucidation of several new criter ia affecting enzyme specificity. Nature and position of the recognized residue, role of adjacent amino acids, lateral chain hydrophobicity, and volume and length of peptides were all considered. Hydrolysis reac tions were also carried out in the presence of glycerol; the effect of microenvironment modifications was quantitative, for example, in indu cing variations in catalytic reaction rates, and also qualitative, suc h as in influencing affinity.