Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies.

Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies. Abstract Text:

T Yamamoto,Y Tonomura,

Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies. Publishing Authors By Initials

T Yamamoto,Y Tonomura,

For similar animal structures: stomach, ruminant: reticulum research abstracts see: animal structures: stomach, ruminant: reticulum research

PUBMED ID PMID:

MEDLINE DATE:

Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 62

Page Numbers: 558-75

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Nov

YEAR: 1967

Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies. Keywords Mesh Terms:

KEYWORDS: Reticulum

MESH TERMS: enzymology

Chemical & Substance for Abstract: Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle I Kinetic studies Related Publications

• A protein factor regulating the state of aggregation of myosin. I. Properties of the factor.
• ATP-induced contraction of sarcomeres.
• Binding of H-meromyosin with F-actin at low ionic strength.
• Binding of p-nitrothiophenol to one glutamic acid residue in the myosin molecule.
• Change in ultraviolet absorption spectrum of H-meromyosin induced by its binding with substrate and competitive inhibitor.
• Changes in biochemical properties of isolated human skeletal myofibrils with age and in Myasthenia gravis.
• Coupling of ATP-hydrolysis with contraction of isolated myofibrillar fragments.
• Dependence of activity of myofibrillar ATPase on sarcomere length and calcium ion concentration.
• Dependence of myofibrillar ATPase activity on sarcomere length.
• G-F transformation of actin and liberation of hydrogen ion.
• On the active site of myosin A-adenosine triphosphatase. VI. Existence of asparaginyl-prolyl-prolyl-lysine near the active site.
• On the active site of myosin A-adenosine triphosphatase. VII. Effect of trinitrophenylation of myosin on the decomposition of phosphoryl myosin.
• Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies.
• Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. II. Intermediate formation of phosphoryl protein.
• Reaction mechanism of the Ca2 plus-dependent ATPase of sarcoplasmic reticulum from skeletal muscle. 3. Ca plus-uptake and ATP-splitting.
• Role of ADP of F-actin in superprecipitation and enzymatic activity of actomyosin.
• Superprecipitation and enzymatic activity of actomyosin as affected by the mode of polymerization and nucleotide of actin.
• Superprecipitation of myosin B caused by ATP as a nucleated growth process.
• Superprecipitation of myosin B induced by ATP as a nucleated growth process.
• The optical rotatory dispersion of myosin A. V. Re-examination of changes in the optical rotatory power of myosin caused by adenosine triphosphate, inorganic pyrophosphate and p-chloro-mercuribenzoate.
• The pre-steady state of the myosin--adenosine triphosphate system. IV. Liberation of ADP from the myosin--ATP system and effects of modifiers on the phosphorylation of myosin.
• The pre-steady state of the myosin-adenosine triphosphate system. 3. Properties of the intermediate.
• The pre-steady state of the myosin-adenosine triphosphate system. 8. Intermediate formation and activation of myosin by ATP.
• The pre-steady state of the myosin-adenosine triphosphate system. I. Initial rapid liberation of inorganic phosphate.
• The pre-steady state of the myosin-adenosine triphosphate system. II. Initial rapid absorption and liberation of hydrogen ion followed by a stopped-flow method.
• The pre-steady state of the myosin-adenosine triphosphate system. IX. Effect of F-actin on the myosin-ATP system.
• The pre-steady state of the myosin-adenosine triphosphate system. V. Evidence for a phosphate exchange reaction between adenosine triphosphate and the "reactive myosin-phosphate complex".
• The pre-steady state of the myosin-adenosine triphosphate system. VI. Effects of ATP concentration, pH and temperature.
• The pre-steady state of the myosin-adenosine triphosphate system. VII. Kinetic studies on the decrease in light-scattering of actomyosin induced by ATP.
• [Properties of a phosphorylated protein as a reaction intermediate of Na+-K+ sensitive ATPase]