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PMID: 5965333 Published · ppublish English Journal Article

Adenosine 5'-triphosphate-arginine phosphotransferase from lobster muscle.

The Biochemical journal ·Vol. 99 ·No. 1 ·1966-04-00 ·Pages 159-61

Virden R, Watts DC

Abstract

1. The amino acid composition of lobster-muscle arginine kinase is given and discussed briefly. 2. The results were used to calculate a partial specific volume of 0.735. 3. The results are compared with the amino acid composition of creatine kinase.

MeSH Terms
Amino Acids/analysis Animals Autoanalysis Crustacea/enzymology Muscles/enzymology Phosphotransferases/analysis
Chemicals
Amino Acids Phosphotransferases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Virden R
Watts D C
References (7)
7 references, click to expand
  1. Adenosine 5'-triphosphate-arginine phosphotransferase from lobster muscle. Molecular weight.
    Biochem J. 1966 Apr;99(1):155-8 PMID: 5965332
  2. The role of thiol groups in the structure and mechanism of action of arginine kinase.
    Biochem J. 1966 Apr;99(1):162-72 PMID: 5965334
  3. Studies on adenosine triphosphate transphosphorylases. II. Amino acid composition of adenosine triphosphate-creatine transphosphorylase.
    J Biol Chem. 1962 Apr;237:1146-54 PMID: 14480256
  4. [THE HETEROGENICITY OF CREATINE KINASE].
    Biochem Z. 1964 Jan 28;339:305-14 PMID: 14126710
  5. ADENOSINE 5'-TRIPHOSPHATE-ARGININE PHOSPHOTRANSFERASE FROM LOBSTER MUSCLE: PURIFICATION AND PROPERTIES.
    Biochem J. 1965 Mar;94:536-44 PMID: 14340045
  6. AN AUTOMATIC TWIN-COLUMN TEN-HOUR AMINO ACID CHROMATOGRAM.
    Anal Biochem. 1965 Aug;12:367-78 PMID: 14342205
  7. AMINO-ACID SEQUENCE AROUND THE REACTIVE THIOL GROUPS OF ADENOSINE TRIPHOSPHATE--CREATINE PHOSPHOTRANSFERASE.
    Nature. 1964 Jul 18;203:267-9 PMID: 14201762
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj0990159
Published
1966-04-00
Pages
159-61
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1264971
Subset
IM
External Links
PubMed source DOI: 10.1042/bj0990159 PMC Full Text View journal details
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