Heterogeneity in enzymatic sites of heavy meromyosin shown by measuring F-actin-inactivated hydrolysis of beta-naphthyl triphosphate.

Heterogeneity in enzymatic sites of heavy meromyosin shown by measuring F-actin-inactivated hydrolysis of beta-naphthyl triphosphate. Research Abstract Details 

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Heterogeneity in enzymatic sites of heavy meromyosin shown by measuring F-actin-inactivated hydrolysis of beta-naphthyl triphosphate. Abstract Text:

H Fujisaki,H Asai,

Enzymatic characteristics of heavy meromyosin (HMM) were investigated by measuring beta-naphthyl triphosphate (beta-NapP3) hydrolysis in the presence and absence of F-actin. beta-NapP3 hydrolysis by HMM was inactivated by F-actin in the presence of Mg ions; in the presence of sufficient F-actin, the activity was about one-half of that in the absence of F-actin. In the presence of Ca ions the activity disappeared almost completely on addition of sufficient F-actin. Two different values of the Michaelis constant (Km) were obtained from the data for beta-NapP3 hydrolysis by HMM in the presence of Mg ions; one of them vanished in the presence of sufficient F-actin, and only one Km value was obtained in the presence of Ca ions. These results suggest the existence of two distinct enzymatic sites in HMM, one inactivated by F-actin in the presence of Mg or Ca ions, the other inactive in the presence of Ca ions but active in the presence of Mg ions and not influenced by F-actin. Use of subfragment-1(A1) (S-1(A1)) and S-1(A2) instead of HMM confirmed that these enzymatic characteristics are not due to a difference in the alkali light chains on myosin heads.

Heterogeneity in enzymatic sites of heavy meromyosin shown by measuring F-actin-inactivated hydrolysis of beta-naphthyl triphosphate. Publishing Authors By Initials

H Fujisaki,H Asai,

For similar organic chemicals: organophosphorus compounds: phosphoric acid esters research abstracts see: organic chemicals: organophosphorus compounds: phosphoric acid esters research

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Heterogeneity in enzymatic sites of heavy meromyosin shown by measuring F-actin-inactivated hydrolysis of beta-naphthyl triphosphate. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 92

Page Numbers: 1577-83

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Nov

YEAR: 1982

Heterogeneity in enzymatic sites of heavy meromyosin shown by measuring F-actin-inactivated hydrolysis of beta-naphthyl triphosphate. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Heterogeneity in enzymatic sites of heavy meromyosin shown by measuring F-actin-inactivated hydrolysis of beta-naphthyl triphosphate. Keywords Mesh Terms:

KEYWORDS: Phosphoric Acid Esters

MESH TERMS: metabolism

Chemical & Substance for Abstract: Heterogeneity in enzymatic sites of heavy meromyosin shown by measuring F-actin-inactivated hydrolysis of beta-naphthyl triphosphate. Information

Substance Name: Calcium

Registry Number: 7440-70-2

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Country: JAPAN

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MEDLINETA: J Biochem

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