It was shown that the heavy chain structure was altered by the phosphorylation of light chain in gizzard myosin. Phosphorylated myosin was compared with unphosphorylated myosin with respect to the chymotryptic fragmentation with or without ATP in the medium. The rise and fall of the fragments were well explained by the reconstitution model for unphosphorylated myosin (Okamoto, Y., et al. (1980) J. Biochem. 88, 361-371). A specific cleavable site in the myosin head was completely abolished by the phosphorylation of light chain. The effect of phosphorylation on the site could be observed in the absence of ATP but not in its presence. These results strongly suggest the possible integrity of the site, 5K daltons apart from the masked N terminus, for the physiological activity of gizzard myosin.
Light chain phosphorylation alters the N terminal structure of gizzard myosin heavy chain in an ATP dependent manner. Publishing Authors By Initials
Light chain phosphorylation alters the N terminal structure of gizzard myosin heavy chain in an ATP dependent manner. Journal Published:
PUBLICATION TYPE: Journal Article
Journal: Journal of biochemistry
VOLUME: 89
Page Numbers: 697-700
Journal Abbreviation: J. Biochem.
ISSN: 0021-924X
DAY: 19
MONTH: Feb
YEAR: 1981
Light chain phosphorylation alters the N terminal structure of gizzard myosin heavy chain in an ATP dependent manner. Information
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LANGUAGE: eng
NlmUniqueID: 376600
Light chain phosphorylation alters the N terminal structure of gizzard myosin heavy chain in an ATP dependent manner. Keywords Mesh Terms:
KEYWORDS: Protein Conformation
MESH TERMS: analysis
Chemical & Substance for Abstract: Light chain phosphorylation alters the N terminal structure of gizzard myosin heavy chain in an ATP dependent manner. Information
Substance Name: Myosins
Registry Number: EC 3.6.1.4
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Country: JAPAN
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MEDLINETA: J Biochem
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