On the mechanism of enzyme action. LXXI. Acylations of trypsin in organic solvents

Journal Article · Thu Sep 01 04:00:00 EDT 1960 · Archives of Biochemistry and Biophysics

DOI:https://doi.org/10.1016/0003-9861(60)90624-X· OSTI ID:4154365

Vratsanos, S. M.

Acetylation of trypsin in dimethyl sulfoxide solutions is a reaction highly specific for the free amino groups of the enzyme. The progressing acetylation causes a gradual reduction of the activity characterized by a complete inactivation upon the introduction of abcut 15 acetyl groups per trypsin molecule. By increasing the bulk of the substituent acyl group, this number is reduced. The inactivation caused by the substitution is apparently associated with a specific configuration that the enzyme assumes in the organic solvent. In formamide the introduction of acetic anhydride results in formylation rather than acetylation. The observation of inactivation in the presence of trypsin competitors for the utilization of the reagent offers a sensitive means of evaluation of the reactivities of various functional groups of proteins.

• Research Organization: Fordham Univ., New York
• Sponsoring Organization: USDOE
• NSA Number: NSA-14-022739
• OSTI ID: 4154365
• Journal Information: Archives of Biochemistry and Biophysics, Journal Name: Archives of Biochemistry and Biophysics Journal Issue: 1 Vol. 90; ISSN 0003-9861
• Country of Publication: Country unknown/Code not available
• Language: English

Related Subjects

ACETYLATION
AMIDES
AMINES
BIOCHEMISTRY
BIOLOGY AND MEDICINE
CHEMICAL REACTIONS
ENZYMES
FREE RADICALS
METHYL RADICALS
PROTEINS
REACTION KINETICS
SENSITIVITY
SOLUTIONS
SOLVENTS
SULFUR OXIDES
TRYPSIN