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.
Full text
PDF


Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BURGER A., RICHTERICH R., AEBI H. DIE HETEROGENITAET DER KREATIN-KINASE. Biochem Z. 1964 Jan 28;339:305–314. [PubMed] [Google Scholar]
- HACKET N., MATHIAS A. P., PENNINGTON F. AN AUTOMATIC TWIN-COLUMN TEN-HOUR AMINO ACID CHROMATOGRAM. Anal Biochem. 1965 Aug;12:367–378. doi: 10.1016/0003-2697(65)90104-1. [DOI] [PubMed] [Google Scholar]
- NOLTMANN E. A., MAHOWALD T. A., KUBY S. A. Studies on adenosine triphosphate transphosphorylases. II. Amino acid composition of adenosine triphosphate-creatine transphosphorylase. J Biol Chem. 1962 Apr;237:1146–1154. [PubMed] [Google Scholar]
- THOMSON A. R., EVELEIGH J. W., MILES B. J. AMINO-ACID SEQUENCE AROUND THE REACTIVE THIOL GROUPS OF ADENOSINE TRIPHOSPHATE--CREATINE PHOSPHOTRANSFERASE. Nature. 1964 Jul 18;203:267–269. doi: 10.1038/203267a0. [DOI] [PubMed] [Google Scholar]
- VIRDEN R., WATTS D. C., BALDWIN E. ADENOSINE 5'-TRIPHOSPHATE-ARGININE PHOSPHOTRANSFERASE FROM LOBSTER MUSCLE: PURIFICATION AND PROPERTIES. Biochem J. 1965 Mar;94:536–544. doi: 10.1042/bj0940536. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Virden R., Watts D. C. The role of thiol groups in the structure and mechanism of action of arginine kinase. Biochem J. 1966 Apr;99(1):162–172. doi: 10.1042/bj0990162. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Virden R., Watts D. C., Watts R. L., Gammack D. B., Raper J. H. Adenosine 5'-triphosphate-arginine phosphotransferase from lobster muscle. Molecular weight. Biochem J. 1966 Apr;99(1):155–158. doi: 10.1042/bj0990155. [DOI] [PMC free article] [PubMed] [Google Scholar]
