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Biomedical subjects

C Turano

Publications and source records attributed to C Turano.

At least 73 records · Page 4Linked to original sources
PubMed1967

Acylation of aspartate aminotransferase.

1. Acetylation of aspartate aminotransferase from pig heart inhibits completely the enzymic activity when the coenzyme is in the amino form (pyridoxamine phosphate) or when the coenzyme has been removed, but not when the coenzyme is in the aldehyde form (pyridoxal phosphate). 2. The group the acylation of which is responsible for the inhibition has been identified with the in-amino group of a lysine residue at the coenzyme-binding site. Moreover, in the pyridoxamine-enzyme the amino group of the coenzyme is also acetylated. 3. The reactivity of the coenzyme-binding lysine residue is greatly different in the pyridoxamine-enzyme and in the apoenzyme, suggesting the possibility of an interaction of its in-amino group with pyridoxamine or with other groups on the protein.

Acetates↗
PubMedDate not supplied

Aspartate aminotransferase from wheat germ: purification and kinetic properties.

A convenient method for the purification of aspartate aminotransferase [L-aspartate-2-oxoglutarate aminotransferase (EC 2.6.1.1)] from wheat germ is described. An overall purification of 150 fold was achieved. On polyacrylamide gel electrophoresis at pH 8.9 the purified enzyme revealed two protein bands both provided with enzymatic activity. The holoenzyme is readily resolved on conversion to the aminic form and gel-filtration. The apoenzyme is reactivated by pyridoxal-5-phosphate. Kinetic data indicate that a Ping-Pong mechanism is operative similar to that found for the tyrosine aminotransferase by Litwack and Cleland (1968). Phosphate ion behaves as a competitive inhibitor towards the coenzyme. The relatively low affinity between coenzyme and apoenzyme from wheat germ allowed the determination of the dissociation constants for coenzymes (pyridoxal-5'-phosphate and pyridoxamine-5'-phosphate) and of the inhibition constant for phosphate.

Aspartate Aminotransferases↗
PubMedDate not supplied

Fucose-carrying nuclear glycoproteins: distribution and tissue specificity.

Glycoproteins recognized by Ulex europaeus lectin I, specific for fucose residues, have been identified in chromatin prepared from pig liver, heart and kidney nuclei. They are present among the proteins dissociated from DNA with salt solutions and, in higher amount, among the proteins dissociated with urea and guanidine. In any case these fucose-containing glycoproteins appear to have a marked tissue specificity, which suggests that they have specific regulatory roles in the processes taking place in the nuclei.

Animals↗