Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect.

Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect. Abstract Text:

H Kuwayama,M Suzuki,R Koga,S Ebashi,

1) Two protein components, 155 and 130 kDa in their electrophoretic molecular weights, respectively, were isolated in a homogeneous state from bovine aorta; they showed both the superprecipitation-inducing effect on desensitized natural actomyosin and the myosin light chain kinase (MLCK) action on gizzard myosin. 2) The superprecipitating activity of the 155 kDa component was 5 time higher than that of the 130 kDa component on the basis of equivalent MLCK activity. 3) The same procedure was applied to bovine stomach, giving rise to a 155 kDa component in a homogeneous state as in the case of aorta, but the 130 kDa component thus prepared was contaminated by higher molecular weight components. 4) If compared on the basis of equivalent MLCK activity, bovine stomach 155 kDa component showed more than 10 times higher superprecipitating activity than the fraction that contained the 130 kDa component as the main constituent. 5) The discrepancy between the superprecipitating activity and MLCK activity mentioned above was discussed in relation to the Ca2+ regulation mechanism in smooth muscle contraction. The possibility that the 130 kDa component might be a proteolytic product of the 155 kDa component was also discussed.

Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect. Publishing Authors By Initials

H Kuwayama,M Suzuki,R Koga,S Ebashi,

For similar digestive system: gastrointestinal tract: upper gastrointestinal tract: stomach research abstracts see: digestive system: gastrointestinal tract: upper gastrointestinal tract: stomach research

PUBMED ID PMID:

MEDLINE DATE:

Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect. Journal Published:

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

Journal: Journal of biochemistry

VOLUME: 104

Page Numbers: 862-6

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Nov

YEAR: 1988

Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect. Keywords Mesh Terms:

KEYWORDS: Stomach

MESH TERMS: enzymology

Chemical & Substance for Abstract: Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect. Information

Substance Name: Myosin-Light-Chain Kinase

Registry Number: EC 2.7.1.117

Grant and Affiliation Information for Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect.

AFFILIATION: National Institute for Physiological Sciences, Aichi.

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect Related Publications

• "M-substance", a new protein constituting the M-line of myofibrils.
• A new simple method of preparing actin from chicken gizzard.
• A simple method of preparing actin-free myosin from smooth muscle.
• ATP-dependent Ca binding of brain microsomes.
• Alpha-actinin, a new structural protein from striated muscle. I. Preparation and action on actomyosinàtp interaction.
• Alpha-actinin, a new structural protein from striated muscle. II. Action on actin.
• Ca-releasing action of beta, gamma-methylene adenosine triphosphate on fragmented sarcoplasmic reticulum.
• Ca2+ regulation in vascular smooth muscle.
• Ca2+ regulation in vascular smooth muscle. II. Ca2+ binding of aorta leiotonin.
• Calcium-induced conformational changes and mutual interactions of troponin components as studied by spin labeling.
• Cardiac troponin.
• Crystallization and preliminary crystallographic data of chicken gizzard G-actin . DNase I complex and Physarum G-actin . DNase I complex.
• Detection of calcium binding proteins by 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis.
• Does phosphorylation of myosin light chain have direct relation to regulation in smooth muscle?
• Effect of phosphates on the structure of the actin filament.
• Essential factor of gizzard "troponin" fraction. A new type of regulatory protein.
• Isolation from bovine brain of 155 kDa component exhibiting myosin light chain kinase activity.
• Localization of 6S component of a alpha-actinin at Z-band.
• Periodic distribution of troponin along the thin filament.
• Preparation of protein components exhibiting myosin light chain kinase activities from bovine aorta: discrepancies between its enzyme activity and actomyosin activating effect.
• Proceedings: Regulation of the myosin-actin interaction by the Ca2+ -troponin-tropomyosin system.
• Requirement of Ca ion for the stimulating effect of cyclic 3',5'-AMP on muscle phosphorylase b kinase.
• Reversible change in physical state of troponin induced by calcium ion.
• Reversible stimulation of muscle phosphorylase b kinase by low concentrations of calcium ions.
• Sea urchin protease specific to the SPKK motif in histone.
• Separation of troponin into its three components.
• Staining of myofibrils with fluorescent antibody against the 10S component of the original alpha-actinin preparation.
• The localization of troponin in tropomyosin paracrystals.
• Troponin and its components.
• Troponin. I. Preparation and physiological function.