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. 1966 Jun;99(3):589–594. doi: 10.1042/bj0990589

Purification and general properties of aspartate aminotransferase of ox heart

G Marino 1,*, Anna Maria Greco 1,*, V Scardi 1,*, R Zito 1
PMCID: PMC1265045  PMID: 6007356

Abstract

1. A five-step procedure for preparing highly purified aspartate aminotransferase from ox heart is described. 2. The homogeneity of the pure enzyme was established by criteria such as ultracentrifugation and electrophoresis in starch gel and in polyacrylamide gel. 3. The pure enzyme has an isoelectric point of about pH5, and E1%1cm. 14·40 at 278mμ. 4. The molecular weight of the pure enzyme was determined as 96000 by sedimentation equilibrium. 5. The pH optimum for the pure enzyme was about 8. It was determined by a new assay technique. 6. A difference in the electrophoretic migration rate between the enzyme from ox heart and brain and the enzyme from pig heart and brain suggests a species specificity rather than an organ specificity. 7. A new effect of deionization on the visible-absorption spectrum of the enzyme was observed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. CAMMARATA P. S., COHEN P. P. Spectrophotometric measurement of transamination reactions. J Biol Chem. 1951 Nov;193(1):45–52. [PubMed] [Google Scholar]
  2. GRIPPO P., IACCARINO M., ROSSI M., SCARANO E. THIN-LAYER CHROMATOGRAPHY OF NUCLEOTIDES, NUCLEOSIDES AND NUCLEIC ACID BASES. Biochim Biophys Acta. 1965 Jan 11;95:1–7. doi: 10.1016/0005-2787(65)90204-2. [DOI] [PubMed] [Google Scholar]
  3. HJERTEN S., LEVIN O., TISELIUS A. Protein chromatography on calcium phosphate columns. Arch Biochem Biophys. 1956 Nov;65(1):132–155. doi: 10.1016/0003-9861(56)90183-7. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. KARMEN A. A note on the spectrometric assay of glutamic-oxalacetic transaminase in human blood serum. J Clin Invest. 1955 Jan;34(1):131–133. [PubMed] [Google Scholar]
  6. LIS H. Purification of glutamic-aspartic transaminase. Biochim Biophys Acta. 1958 Apr;28(1):191–197. doi: 10.1016/0006-3002(58)90446-3. [DOI] [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. 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]
  9. Marino G., Greco A. M., Scardi V. Un semplice e sensibile metodo per misurare l'attività transaminasica. Boll Soc Ital Biol Sper. 1965 Dec 31;41(24):1577–1580. [PubMed] [Google Scholar]
  10. Marino G., Scardi V., Zito R. Amino acid composition and terminal residues of aspartate aminotransferase from ox heart. Biochem J. 1966 Jun;99(3):595–598. doi: 10.1042/bj0990595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Marino G., Zito R., Scardi V. Aspartato aminotransferasi da cervello bovino. II. Proprieta. Boll Soc Ital Biol Sper. 1964 Jun 30;40(12):720–721. [PubMed] [Google Scholar]
  12. SCARDI V., SCOTTO P., IACCARINO M., SCARANO E. The binding of pyridoxal 5-phosphate to aspartate aminotransferase of pig heart. Biochem J. 1963 Jul;88:172–175. doi: 10.1042/bj0880172. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. SMITHIES O. Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults. Biochem J. 1955 Dec;61(4):629–641. doi: 10.1042/bj0610629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. WADA H., SNELL E. E. Enzymatic transamination of pyridoxamine. I. With oxaloacetate and alpha-ketoglutarate. J Biol Chem. 1962 Jan;237:127–132. [PubMed] [Google Scholar]

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