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Title: Direct photoaffinity labeling by nucleotides of the apparent catalytic site on the heavy chains of smooth muscle and Acanthamoeba myosins

Abstract

The heavy chains of Acanthamoeba myosins, IA, IB and II, turkey gizzard myosin, and rabbit skeletal muscle myosin subfragment-1 were specifically labeled by radioactive ATP, ADP, and UTP, each of which is a substrate or product of myosin ATPase activity, when irradiated with uv light at 0/sup 0/C. With UTP, as much as 0.45 mol/mol of Acanthamoeba myosin IA heavy chain and 1 mol/mol of turkey gizzard myosin heavy chain was incorporated. Evidence that the ligands were associated with the catalytic site included the observations that reaction occurred only with nucleotides that are substrates or products of the ATPase activity; that the reaction was blocked by pyrophosphate which is an inhibitor of the ATPase activity; that ATP was bound as ADP; and that label was probably restricted to a single peptide following limited subtilisin proteolysis of labeled Acanthamoeba myosin IA heavy chain and extensive cleavage with CNBr and trypsin of labeled turkey gizzard myosin heavy chain.

Authors:
;
Publication Date:
OSTI Identifier:
6172038
Resource Type:
Journal Article
Journal Name:
J. Biol. Chem.; (United States)
Additional Journal Information:
Journal Volume: 256:1
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; 59 BASIC BIOLOGICAL SCIENCES; MYOSIN; LABELLING; PHOTOCHEMICAL REACTIONS; ADP; AMOEBA; AMP; ATP; ATP-ASE; ENZYME ACTIVITY; ENZYME INHIBITORS; FOWL; METABOLISM; MUSCLES; NUCLEOTIDES; PEPTIDES; PYROPHOSPHATES; RABBITS; SUBSTRATES; TRYPSIN; ULTRAVIOLET RADIATION; ACID ANHYDRASES; ANIMALS; BIRDS; CHEMICAL REACTIONS; ELECTROMAGNETIC RADIATION; ENZYMES; GLOBULINS; HYDROLASES; INVERTEBRATES; MAMMALS; MICROORGANISMS; ORGANIC COMPOUNDS; OXYGEN COMPOUNDS; PEPTIDE HYDROLASES; PHOSPHOHYDROLASES; PHOSPHORUS COMPOUNDS; PROTEINS; PROTOZOA; RADIATIONS; SARCODINA; SERINE PROTEINASES; VERTEBRATES; 560111* - Radiation Effects on Biochemicals- In Vitro- (-1987); 550200 - Biochemistry

Citation Formats

Maruta, H., and Korn, E.D. Direct photoaffinity labeling by nucleotides of the apparent catalytic site on the heavy chains of smooth muscle and Acanthamoeba myosins. United States: N. p., 1981. Web.
Maruta, H., & Korn, E.D. Direct photoaffinity labeling by nucleotides of the apparent catalytic site on the heavy chains of smooth muscle and Acanthamoeba myosins. United States.
Maruta, H., and Korn, E.D. Sat . "Direct photoaffinity labeling by nucleotides of the apparent catalytic site on the heavy chains of smooth muscle and Acanthamoeba myosins". United States.
@article{osti_6172038,
title = {Direct photoaffinity labeling by nucleotides of the apparent catalytic site on the heavy chains of smooth muscle and Acanthamoeba myosins},
author = {Maruta, H. and Korn, E.D.},
abstractNote = {The heavy chains of Acanthamoeba myosins, IA, IB and II, turkey gizzard myosin, and rabbit skeletal muscle myosin subfragment-1 were specifically labeled by radioactive ATP, ADP, and UTP, each of which is a substrate or product of myosin ATPase activity, when irradiated with uv light at 0/sup 0/C. With UTP, as much as 0.45 mol/mol of Acanthamoeba myosin IA heavy chain and 1 mol/mol of turkey gizzard myosin heavy chain was incorporated. Evidence that the ligands were associated with the catalytic site included the observations that reaction occurred only with nucleotides that are substrates or products of the ATPase activity; that the reaction was blocked by pyrophosphate which is an inhibitor of the ATPase activity; that ATP was bound as ADP; and that label was probably restricted to a single peptide following limited subtilisin proteolysis of labeled Acanthamoeba myosin IA heavy chain and extensive cleavage with CNBr and trypsin of labeled turkey gizzard myosin heavy chain.},
doi = {},
journal = {J. Biol. Chem.; (United States)},
number = ,
volume = 256:1,
place = {United States},
year = {1981},
month = {1}
}