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Macrophages contain at least two myosins
Author(s) -
Trotter John A.,
Scordilis Stylianos P.,
Margossian Sarkis S.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80264-6
Subject(s) - myosin , immunoglobulin light chain , myosin light chain kinase , polyacrylamide gel electrophoresis , chemistry , electrophoresis , gel electrophoresis , biochemistry , microbiology and biotechnology , biology , antibody , immunology , enzyme
A number of motile functions of macrophages are thought to be mediated by myosin. We have observed that myosin from rabbit alveolar macrophages is heterogeneous with respect to its 20 kDa light chain: two species of 20 kDa light chain are identified by one‐dimensional and two‐dimensional polyacrylamide gel electrophoresis, in a ratio of 2:1. Native myosin, analyzed on non‐denaturing gels, is also composed of two species, in a ratio of 2:1. These results indicate that macrophages contain at least two different myosins, which might have different physiological functions.