The steady state intermediate of scallop smooth muscle myosin ATPase and effect of light chain phosphorylation. A molecular mechanism for catch contraction.

The steady state intermediate of scallop smooth muscle myosin ATPase and effect of light chain phosphorylation. A molecular mechanism for catch contraction. Research Abstract Details 

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The steady state intermediate of scallop smooth muscle myosin ATPase and effect of light chain phosphorylation. A molecular mechanism for catch contraction. Abstract Text:

M Takahashi,H Sohma,F Morita,

The ATP-induced difference UV-absorption spectrum of myosin isolated from the opaque portion of scallop smooth muscle (opaque myosin) was Ca2+-sensitive at 40 mM KCl and 1.5 M sucrose. On adding sucrose to 1.5 M, the turbidity of myosin decreased to 24% and the characteristic two forms of the difference spectrum, the ATP-form and ADP-form (Morita, F. (1967) J. Biol. Chem. 242, 4501-4506), were distinguishable. In the presence of Ca2+, the difference spectrum was the ATP-form first and then decayed into the ADP-form with the depletion of ATP. In the absence of Ca2+, however, only the ADP-form was observed. The ADP-form observed in the absence of Ca2+ returned to the ATP-form when the regulatory light chain-a (RLC-a), one of the regulatory light chains of opaque myosin, was phosphorylated. These results suggest that the main intermediate at the steady state of opaque myosin ATPase is converted depending on the concentration of Ca2+, from EPADP in the presence of Ca2+ to EADP in the absence of Ca2+. It changes to EPADP in the absence of Ca2+ on the phosphorylation of RLC-a. Consistent results were obtained by measuring the ATP-induced Trp-fluorescence increase of opaque myosin in the absence of sucrose. Since the opaque portion of scallop smooth muscle is known to be responsible for catch contraction (Ruegg, J.C. (1961) Proc. R. Soc. London Ser. B 154, 224-249), these findings lead us to suppose that the opaque myosin in vivo may stay in the E.ADP complex during the catch state. It changes to EPADP by the phosphorylation of RLC-a, which may terminate the catch state.

The steady state intermediate of scallop smooth muscle myosin ATPase and effect of light chain phosphorylation. A molecular mechanism for catch contraction. Publishing Authors By Initials

M Takahashi,H Sohma,F Morita,

For similar inorganic chemicals: elements: metals, alkali: potassium research abstracts see: inorganic chemicals: elements: metals, alkali: potassium research

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The steady state intermediate of scallop smooth muscle myosin ATPase and effect of light chain phosphorylation. A molecular mechanism for catch contraction. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 104

Page Numbers: 102-7

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1988

The steady state intermediate of scallop smooth muscle myosin ATPase and effect of light chain phosphorylation. A molecular mechanism for catch contraction. Information

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LANGUAGE: eng

NlmUniqueID: 376600

The steady state intermediate of scallop smooth muscle myosin ATPase and effect of light chain phosphorylation. A molecular mechanism for catch contraction. Keywords Mesh Terms:

KEYWORDS: Potassium

MESH TERMS: pharmacology

Chemical & Substance for Abstract: The steady state intermediate of scallop smooth muscle myosin ATPase and effect of light chain phosphorylation. A molecular mechanism for catch contraction. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for The steady state intermediate of scallop smooth muscle myosin ATPase and effect of light chain phosphorylation. A molecular mechanism for catch contraction.

AFFILIATION: Department of Chemistry, Faculty of Science, Hokkaido University.

Country: JAPAN

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MEDLINETA: J Biochem

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