Synthesis of monosulfates of unconjugated and conjugated bile acids.
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Biomedical subjects
Publications and source records attributed to F Hasegawa.
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Microsomal squalene epoxidase has previously been solubilized with Triton X-100 and resolved into fractions, FA and FB, by DEAE-cellulose chromatography (Ono T. and Bloch K (1975) J biol. Chem. 250, 1571-1579). It has now been found that FB is identical with NADPH-cytochrome c reductase (denoted FPT, EC 1.6.2.3). Although both NADPH and NADH served as electron donors, the former was preferred for squalene epoxidase activity in the reconstituted system of FA and FB. FB is characterized by its ability to reduce cytochrome c by NADPH. In place of FB, partially purified FPT was tested for its ability to support squalene epoxidation in the presence of FA. A stepwise purification of the deoxycholate-solubilized FPT yielded an increase in specific FPT activity with a parallel increase in squalene epoxidase activity. Bromelain-solubilized FPT was less effective. Rabbit antisera preparations to the purified FPT solubilized with trypsin were shown to inhibit concomitantly FPT activity and squalene epoxidase activity. These observations support the concept that squalene epoxidation is primarily mediated via a flavoprotein, NADPH-cytochrome c reductase, and a terminal oxidase, squalene epoxidase, which is distinct from cytochrome P-450.
A method was developed to isolate transitional cells from the mucous lining of the rat urinary bladder by treatment with ethylene diaminetetraacetic acid and sonication. The isolated cells were examined by phase contrast microscopy, Giemsa staining, and scanning electron microscopy. Two types of isolated cells were distinguished: large ones which were characterized as superficial cells and smaller ones which seemed to be intermediate basal cells.
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