Abstract
1. The influence of Cl−, Br−, NO3− and F− ions on the visible-absorption spectrum of deionized aspartate aminotransferase was investigated. 2. Except for F−, these anions caused an increase of the extinction at 430mμ with a concomitant decrease of that at 362mμ. 3. The affinity constants for Cl− and NO3− ions were calculated by a procedure based on the assumption that the anion stabilizes the protonated form of the enzyme chromophore (λmax. 430mμ). 4. The true pK of the chromophore of the enzyme was found to be 5·25.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- JENKINS W. T., YPHANTIS D. A., SIZER I. W. Glutamic aspartic transaminase. I. Assay, purification, and general properties. J Biol Chem. 1959 Jan;234(1):51–57. [PubMed] [Google Scholar]
- Marino G., Greco A. M., Scardi V. Purificazione di aspartato aminotransderasi da cuore bovino. Boll Soc Ital Biol Sper. 1965 Apr 30;41(8):438–440. [PubMed] [Google Scholar]
- Marino G., Greco A. M., Scardi V., Zito R. Purification and general properties of aspartate aminotransferase of ox heart. Biochem J. 1966 Jun;99(3):589–594. doi: 10.1042/bj0990589. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Martinez-Carrion M., Turano C., Chiancone E., Bossa F., Giartosio A., Riva F., Fasella P. Isolation and characterization of multiple forms of glutamate-asparate aminotransferase from pig heart. J Biol Chem. 1967 May 25;242(10):2397–2409. [PubMed] [Google Scholar]