Literature DB >> 13192074

Adenosinetriphosphate-creatine transphosphorylase. II. Homogeneity and physicochemical properties.

L NODA, S A KUBY, H A LARDY.   

Abstract

Keywords:  MUSCLES/metabolism; TRANSPHOSPHORYLASES

Mesh：

Substances：

Year:  1954        PMID： 13192074

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


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  17 in total

1.  STUDIES ON THE MECHANISM OF ACTION OF ADENOSINE 5'-TRIPHOSPHATE-CREATINE PHOSPHOTRANSFERASE. INHIBITION BY MANGANESE IONS AND BY P-NITROPHENYL ACETATE.

Authors:  D C WATTS
Journal:  Biochem J       Date:  1963-11       Impact factor: 3.857

2.  [ON THE LOCALIZATION OF CREATINE KINASE (CK) IN MITOCHONDRIA AND MICROSOMES IN HUMAN SKELETAL MUSCLES, MYOCARDIUM AND CEREBRAL CORTEX].

Authors:  T O KLEINE
Journal:  Klin Wochenschr       Date:  1965-05-01

3.  The conversion of adenosine 5'-phosphate into adenosine triphosphate as catalysed by adenosine triphosphate--creatine phosphotransferase and adenosine triphosphate--adenosine monophosphate phosphotransferase in the presence of phosphocreatine.

Authors:  M D DOHERTY; J F MORRISON
Journal:  Biochem J       Date:  1963-02       Impact factor: 3.857

4.  Adenosine triphosphate-creatine phosphotransferase from ox brain: purification and isolation.

Authors:  T WOOD
Journal:  Biochem J       Date:  1963-06       Impact factor: 3.857

5.  A study of the 'reactive' sulphydryl groups of adenosine 5'-triphosphate-creatine phosphotransferase.

Authors:  D C WATTS; B R RABIN
Journal:  Biochem J       Date:  1962-12       Impact factor: 3.857

6.  Studies on the proteins of fish skeletal muscle. 5. Molecular weight and shape of cod fibrillar proteins.

Authors:  J J CONNELL
Journal:  Biochem J       Date:  1958-09       Impact factor: 3.857

7.  The number of catalytic sites in creatine phosphokinase as determined by a study of its reactive sulphydryl groups.

Authors:  D C Watts; B R Rabin; E M Crook
Journal:  Biochem J       Date:  1962-03       Impact factor: 3.857

8.  A change in optical rotation of creatine-ATP transphosphorylase during enzyme substrate interaction suggesting an alteration in conformation.

Authors:  A J SAMUELS; T NIHEI; L NODA
Journal:  Proc Natl Acad Sci U S A       Date:  1961-12-15       Impact factor: 11.205

9.  Inhibition of adenosine 5'-triphosphate-creatine phosphotransferase by substrate-anion complexes. Evidence for the transition-state organization of the catalytic site.

Authors:  E J Milner-White; D C Watts
Journal:  Biochem J       Date:  1971-05       Impact factor: 3.857

10.  Brain adenosine 5'-triphosphate-creatine phosphotransferase.

Authors:  R S Atherton; J F Laws; B J Miles; A R Thomson
Journal:  Biochem J       Date:  1970-12       Impact factor: 3.857
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