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Immunological properties of myosin light-chain kinases.

Authors
Type
Published Article
Journal
Biochimica et Biophysica Acta
0006-3002
Publisher
Elsevier
Publication Date
Volume
914
Issue
1
Pages
74–82
Identifiers
PMID: 3111536
Source
Medline
License
Unknown

Abstract

We have studied the immunological and structural properties of myosin light-chain kinases. Immunological studies were performed with affinity-purified antibodies to turkey gizzard smooth-muscle myosin light-chain kinase. Immunoprecipitation experiments demonstrated that avian smooth muscles contain a myosin light-chain kinase of Mr 130,000, whereas the enzyme immunoprecipitated from canine smooth muscles tested has an Mr of 150,000. These antibodies do not react with cardiac- or skeletal-muscle myosin light-chain kinases. Experiments performed with myosin light-chain kinases purified from turkey gizzards (Mr 130,000), bovine tracheal smooth muscle (Mr 160,000) and human platelets (Mr 100,000) demonstrated the following: the primary structures of the turkey gizzard and bovine tracheal enzymes appear to be quite different, based on one-dimensional peptide maps; only one-third as many antibodies bind to the bovine tracheal enzyme as compared to the turkey gizzard enzyme; the antibody:myosin light-chain kinase ratios for half-maximal inhibition of all three enzymes are similar. Based on these data, we conclude that myosin light-chain kinases constitute an immunologically and structurally heterogeneous group of enzymes that have certain catalytic and regulatory properties in common.

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