title: Purification and characterization of alkaline phosphatase from human seminomas.
abstract: Despite the apparent link between the presence of alkaline phosphatase (ALP) and various cancers, it has so far been difficult to determine distinct differences between seminoma-derived ALP and placental ALP (PLAP). In order to determine specificity, we purified ALP from a seminoma type of human testicular cancer tissue and compared its biochemical and immunological properties with those of PLAP. The purified ALP had a specific activity of 66 units per mg of protein, and it was possible to obtain 169 microg of purified preparation from 60 g of tissue. The molecular weight of the purified seminoma enzyme was approximately 500 kDa. We found that a novel type of ALP from human testicular cancer tissue exists, with a high molecular weight and differing in degree, from the seminoma ALP previously reported.
authors.affiliation: Natural Products Research Department, Teikoku Hormone Mfg. Co., Ltd., Japan.
authors.forename: T
authors.initials: T
authors.lastname: Yamamoto
authors.forename: Y
authors.initials: Y
authors.lastname: Katsuoka
mesh_terms: D000328:Adult; D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors / Q000276:immunology / Q000302:isolation & purification*; D006801:Humans; D008297:Male; D008970:Molecular Weight; D018239:Seminoma / Q000201:enzymology* / Q000473:pathology; D013736:Testicular Neoplasms / Q000201:enzymology* / Q000473:pathology
chemical_list: D000469:Alkaline Phosphatase