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T R Boyde

Publications and source records attributed to T R Boyde.

29 records · Page 2Linked to original sources

The interaction between alpha-2-macroglobulin and cationic aspartate aminotransferase.

On starch-gel or polyacrylamide-gel electrophoresis of human serum, a supernumerary zone of aspartate aminotransferase activity may be demonstrated, migrating with the slow alpha(2) protein zone. This appearance is due only to cationic aspartate aminotransferase, bound by alpha(2)-macroglobulin. The binding is strongly potentiated by dilute borate buffers.

Acrylates↗

Aspartate aminotransferase. The effects of ionic concentration of kinetic constants of both isoenzymes.

1. The Michaelis constants for both isoenzymes for both substrates depend strongly on ionic concentration, being approximately proportional to phosphate concentration over considerable ranges. This is probably an effect of anions only. 2. In the absence of added salt, K(m) (2-oxoglutarate) (anionic isoenzyme) is so small as to be indeterminate. 3. K(m) (l-aspartate) (anionic isoenzyme) passes through a sharp minimum at about 3.3mm-phosphate. It is not clear whether this is a specific effect of phosphate. 4. Both substrates are inhibitory at sufficiently low ionic concentrations. 5. A modified graphical procedure is described for the derivation of the kinetic constants.

Aspartate Aminotransferases↗