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A new variant of the placental acid phosphatases: its implications regarding their subunit structures and genetical determination

BIultiple acid phosphatase isozymes active towards the substrate sodium a-naphthyl phosphate have been described in human tissue extracts by several groups of investigators (e.g. Lundin & Allison, 1966a, b ; Beckman & Beckman, 1967; Rozenszajn, Epstein & Shoham, 1968; Beckman et al. (1968); Smith & Whitby, 1968; Beckman, Beckman & Tarnvik (1970); Li, Yam & Lam 1970). Beckman and colleagues reported a rare electrophoretic variant in placenta affecting two of the three main acid phosphatase isozymes of this tissue. This was interpreted as the heterozygous expression of a rare gene determining a polypeptide subunit found in both isozymes. Family studies were done using leucocytes and the inheritance of this variant pattern was confirmed. In the present paper we report a new variant of placental acid phosphatase which also affects two of the main isozymes but only one of these corresponds to those affected in the previously reported variant. The results suggest that a different gene locus is involved, and provide further information as to the subunit structure of the isoenzymes. We also report studies on the molecular size, thermostability, electrophoretic changes on storage and other properties of these acid phosphatases.