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Identification of two forms of myosin light chain kinase in turkey gizzard
Author(s) -
Walsh Michael P.,
Hinkins Susan,
Muguruma Michio,
Hartshorne David J.
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)80138-0
Subject(s) - gizzard , myosin light chain kinase , immunoglobulin light chain , myosin , identification (biology) , chain (unit) , chemistry , biophysics , biochemistry , biology , botany , genetics , physics , ecology , antibody , astronomy
Two forms of myosin light chain kinase from turkey gizzard are separable by ion‐exchange chromatography. One is the well‐characterized 13 000 M r enzyme. Purification of the second form by affinity chromatography on calmodulin‐Sepharose showed it to consist of two polypeptide chains of M r 136 000 and 141 000. This form of the enzyme required Ca 2+ and calmodulin for activity, was specific for the M r 20 000 light chain of myosin, and appeared to phosphorylate the same site on the light chain as the M r 130 000 enzyme. The low‐ M r gizzard kinase may be a proteolytic fragment of a higher‐ M r species or these may represent different isoenzymes.