Literature DB >> 13211664

Mechanism of hydrolysis of adenosinetriphosphate catalyzed by purified muscle proteins.

D E KOSHLAND, Z BUDENSTEIN, A KOWALSKY.   

Abstract

Entities:  

Keywords:  ADENYLPYROPHOSPHATE; MUSCLE PROTEINS

Mesh：

Substances：

Year:  1954        PMID： 13211664

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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  5 in total

1.  [THE DETERMINATION OF THE ABSOLUTE TURNOVER RATES OF ATP, CREATINE PHOSPHATE AND ORTHOPHOSPHATE IN THE RESTING SKELETAL MUSCLE WITH THE USE OF O-18-LABELED H2O AS A TRACER].

Authors:  J JANKE; P MARMIER; A FLECKENSTEIN
Journal:  Pflugers Arch Gesamte Physiol Menschen Tiere       Date:  1965

2.  The phosphotransferase activity of phosphatases. 2. Studies with purified alkaline phosphomonoesterases and some substrate-specific phosphatases.

Authors:  R K MORTON
Journal:  Biochem J       Date:  1958-09       Impact factor: 3.857

3.  The inhibition of enzymes by beryllium.

Authors:  M Thomas; W N Aldridge
Journal:  Biochem J       Date:  1966-01       Impact factor: 3.857

4.  Phosphate binding by cerebral microsomes in relation to adenosine-triphosphatase activity.

Authors:  R Rodnight; D A Hems; B E Lavin
Journal:  Biochem J       Date:  1966-11       Impact factor: 3.857

5.  Separation of adenosine diphosphate--adenosine triphosphate-exchange activity from the cerebral microsomal sodium-plus-potassium ion-stimulated adenosine triphosphatase.

Authors:  W L Stahl; A Sattin; H McIlwain
Journal:  Biochem J       Date:  1966-05       Impact factor: 3.857
  5 in total

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