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Biomedical subjects

V Scardi

Publications and source records attributed to V Scardi.

31 records · Page 2Linked to original sources
PubMed1968

The influence of chloride and other univalent inorganic anions on the visible-absorption spectrum of aspartate aminotransferase.

1. The influence of Cl(-), Br(-), NO(3) (-) 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 430mmu with a concomitant decrease of that at 362mmu. 3. The affinity constants for Cl(-) and NO(3) (-) ions were calculated by a procedure based on the assumption that the anion stabilizes the protonated form of the enzyme chromophore (lambda(max.) 430mmu). 4. The true pK of the chromophore of the enzyme was found to be 5.25.

Aspartate Aminotransferases↗
PubMed1966

Purification and general properties of aspartate aminotransferase of ox heart.

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.

Animals↗
PubMed1966

Amino acid composition and terminal residues of aspartate aminotransferase from ox heart.

1. The amino acid composition of highly purified aspartate aminotransferase from ox heart was determined. 2. Alanine is the only N-terminal residue. 3. Leucine was identified as the only C-terminal residue. 4. No disulphide bridges are present in the enzyme molecule. 5. The thiol groups are not equally accessible, the accessibility being comparatively easier in the apoenzyme molecule.

Amino Acids↗