Initial rates of peptide‐bond synthesis catalyzed by poly (ethylene glycol)‐modified
chymotrypsin in benzene were determined using high‐performance liquid chromatography …

The substrate specificities of α-chymotrypsin and subtilisins for peptide synthesis in
hydrophilic organic solvents were investigated. Chymotrypsin exhibited high specificity to …

The ratio of the initial rates of aminolysis and hydrolysis in peptide semisynthesis catalyzed
by chymotrypsin (EC 3.4. 21.1) and trypsin (EC 3.4. 21.4) was found to depend non-linearly …

Chymotrypsin was modified in the zymogen form with 2, 4‐bis (O‐methoxypolyethylene
glycol)‐6‐chloro‐s‐triazine (activated PEG2), followed by activation with trypsin. The …

Chymotrypsin modified with polyethylene glycol was successfully used for peptide synthesis
in organic solvents. The benzene‐soluble modified enzyme readily catalyzed both …

The mechanism of peptide semisynthesis catalyzed by α-chymotrypsin and β-trypsin has
been investigated. The dependence of the apparent ratio of the second order rate constants …

The catalytic feature of serine proteases for synthetic reactions in hydrophilic organic
solvents and effects of immobilization by complexation with polysaccharides are described …

Serineand cysteine proteases (trypsin, chymotrypsin, papain, subtilisin) in the presence of
certain concentrations of water-miscible organic solvents express no amidase activities. The …

Calculation of kinetic constants of an enzymatic reaction in organic solvents requires
knowledge of the functional active‐site concentration in organic solvents, and this can be …

The steady-state kinetic parameters of the tripeptides d-Val-Leu-Lys-, Ala-Phe-Lys-, and<
Glu-Phe-Lys-in which the free carboxyl group was substituted with p-nitroaniline (substrate) …