Literature DB >> 5494223

Preparation and properties of creatine kinase from the breast muscle of normal and dystrophic chicken (Gallus domesticus).

B P Roy, J F Laws, A R Thomson.   

Abstract

1. The purification of creatine kinase from normal and genetically dystrophic chicken breast muscle is described. Enzyme recovery was significantly lower from dystrophic muscle. 2. Both enzymes had the same number of reactive and total thiol groups and had similar specific activities and similar amino acid compositions. 3. No significant differences were observed in sedimentation, electrophoretic or kinetic properties. 4. Peptide ;maps' showed no significant differences, and electrophoresis of partial acid hydrolysates of the labelled enzymes suggested that corresponding amino acid sequences around all the thiol groups were very similar. 5. The enzymes showed identical temperature stabilities. 6. No significant differences between the enzymes from normal and dystrophic muscle were observed.

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Year:  1970        PMID: 5494223      PMCID: PMC1179582          DOI: 10.1042/bj1200177

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  19 in total

1.  THE ONTOGENY OF CREATINE KINASE ISOZYMES.

Authors:  H M EPPENBERGER; M EPPENBERGER; R RICHTERICH; H AEBI
Journal:  Dev Biol       Date:  1964-08       Impact factor: 3.582

2.  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

3.  FACTORS INFLUENCING THE CONCENTRATION OF ENZYMES IN VARIOUS MUSCLES.

Authors:  D M DAWSON; N O KAPLAN
Journal:  J Biol Chem       Date:  1965-07       Impact factor: 5.157

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.  Dystrophia Muscularis: A HEREDITARY PRIMARY MYOPATHY IN THE HOUSE MOUSE.

Authors:  A M Michelson; E S Russell; P J Harman
Journal:  Proc Natl Acad Sci U S A       Date:  1955-12-15       Impact factor: 11.205

7.  Further evidence for the role of the essential thiol groups in adenosine triphosphate-creatine phosphotransferase from a comparison of the human and rabbit enzymes.

Authors:  D C Watts; I Kumudavalli
Journal:  Biochem J       Date:  1970-06       Impact factor: 3.857

8.  The comparative enzymology of creatine kinases. I. Isolation and characterization from chicken and rabbit tissues.

Authors:  H M Eppenberger; D M Dawson; N O Kaplan
Journal:  J Biol Chem       Date:  1967-01-25       Impact factor: 5.157

9.  Enzymatic adaptation to contractile activity in skeletal muscle.

Authors:  J Kendrick-Jones; S V Perry
Journal:  Nature       Date:  1965-12-11       Impact factor: 49.962

10.  Properties and reaction with iodoacetamide of adenosine 5'-triphosphate-creatine phosphotransferase from human skeletal muscle. Further evidence about the role of the essential thiol group in relation to the mechanism of action.

Authors:  I Kumudavalli; B H Moreland; D C Watts
Journal:  Biochem J       Date:  1970-04       Impact factor: 3.857

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  3 in total

1.  A protein that binds specifically to the M-line of skeletal muscle is identified as the muscle form of creatine kinase.

Authors:  D C Turner; T Wallimann; H M Eppenberger
Journal:  Proc Natl Acad Sci U S A       Date:  1973-03       Impact factor: 11.205

2.  Purification and properties of adenosine triphosphate-creatine phosphotransferase from muscle of the dogfish Scylliorhinus canicula.

Authors:  B Simonarson; D C Watts
Journal:  Biochem J       Date:  1972-08       Impact factor: 3.857

3.  The amino acid sequence of the peptide containing the thiol group of creatine kinase from normal and dystrophic chicken breast muscle. Comparison of some of the immunological properties of the antibodies developed in rabbits against these enzymes.

Authors:  B P Roy
Journal:  Biochem J       Date:  1974-10       Impact factor: 3.857

  3 in total

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