Abstract

1. 1. A homogeneous, tartrate-inhibitable acid phosphatase (AcPase) was obtained from the liver of channel catfish ( Ictalurus punctatus) by the use of Affi Gel-10-coupled aminohexyltartramic acid affinity chromatography. 2. 2. The enzyme has a molecular weight of 82,500 and is a dimer consisting of two apparently equivalent subunits with subunit weights of 35,000 ± 3000. Amino acid composition data are presented and compared with those of mammalian acid phosphatases. 3. 3. Data suggest that the enzyme is a metalloacid phosphatase. 4. 4. Catfish liver AcPase exhibits two molecular forms with pI 5.66 and 5.37 which were separated by chromatofocusing. 5. 5. A spontaneous conversion of the less acidic form to a more acidic form was observed and this conversion was accompanied by a decreased sensitivity towards tartrate inhibition.

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