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PMID: 6007356 Published · ppublish English Journal Article

Purification and general properties of aspartate aminotransferase of ox heart.

The Biochemical journal ·Vol. 99 ·No. 3 ·1966-06-00 ·Pages 589-94

Marino G, Greco AM, Scardi V, Zito R

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 E(1%) (1cm.) 14.40 at 278mmu. 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.

MeSH Terms
Animals Aspartate Aminotransferases/analysis Carbon Isotopes Cattle Centrifugation, Density Gradient Chromatography Electrophoresis Hydrogen-Ion Concentration Molecular Weight Myocardium/enzymology Ultracentrifugation
Chemicals
Carbon Isotopes Aspartate Aminotransferases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Marino G
Greco A M
Scardi V
Zito R
References (14)
14 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1966-06-00
Pages
589-94
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1265045
Subset
IM
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