Glutamic‐Aspartic Transaminase — Antitransaminase Interaction:

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Abstract
Transaminase was cross‐linked with various proteins after the addition of glutaraldehyde or ethyl chloroformate. The water insoluble conjugates were used for the purification of antitransaminase and antiapotransaminase. A method is described. Pig heart transaminase and ox heart transaminase react differently with anti‐pig‐heart transaminase and apotransaminase. Slight differences were also observed in the reactions between holoenzyme and apoenzyme with their homologous and heterologous antibodies. l‐Aspartate and α‐ketoglutarate protect transaminase from the inhibitory action of antitransaminase. Pyridoxal‐5′‐phosphate has no effect on the enzyme‐antienzyme binding when added in the system in stoichiometric amounts. Higher concentrations of the coenzyme, however, activate the complex antigen‐antibody by facilitating its solubilization. The intact conformation of transaminase is not essential for enzyme‐antienzyme‐binding. Peptides in the dialysate of a tryptic or a chymotryptic hydrolysate of transaminase were able to react with the antibody and form a precipitate.

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