Abstract

Abstract Four staining methods for aspartate aminotransferase (AAT) detection after electrophoresis have been reported. Comparison of the minimum AAT activity detected by these methods showed the following sequence: Sakakibara et al.> Rej and Herder > Decker and Rau > Banks et al. Addition of ADP and diaphorase to the stain of Banks increased its sensitivity 10 fold. The presence of lactate dehydrogenase (LDH > activity in the samples gave electrophoretical artifacts when the methods of Banks et al. and Rej & HoSrder were used. These artifacts were due to the nothing dehydrogenase (NoDH) activity of LDH as demonstrated by chromatography on 5′ AMP-Sepharose 4B (LDH affinity support). Comparative studies were carried out with cytosolic AATases from human, rat and chicken livers. The methods which used cystains sulfinic acid as amino donor (Sakakibara et al.) or Fast Violet B as stain (Decker & Rau) were the sole really specific for the evaluation of AAT activity in biological extracts.

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