Cytosolic aspartate aminotransferases from chicken heart, liver, spleen, skeletal muscle and breast muscle differed in number of their molecular forms, detected by polyacrylamide gel electrophoresis and specific staining. The number of molecular forms varied from tissue to tissue but the electrophoretic mobilities of a given form in all tissues were analogous. Within a single tissue most of the enzyme activity was present as the lowest-running band (alpha form) and the rest was distributed in minor bands termed (B,tau, alpha and epsilon forms). We report a method for the purification of cytosolic aspartate aminotransferases from various chicken tissues. The procedure can be carried out in one week and allows the obtention of isolated molecular forms of the enzyme, independently of the tissue under study. Separation of multiple forms was also achieved by chromatofocusing. The isoelectric points determined by this method for a given form in all five tissues were analogous and differed from those of the molecular forms of the enzyme from other origins. An Mr of 100,000 was obtained for all molecular forms of the five chicken tissues studied.