[Purification of lipase of microbial origin by silochrome chromatography].

The possibility of purifying lipase from Geotrichum asteroides by chromatography with a modified silochrome used as sorbent has been explored. The paper presents a scheme of adsorption and subsequent desorption of lipase from octylsilochrome which requires that ethylene glycol, Na-deoxycholate and Triton X-100 be used as eluents. Triton, the last in the sequence, eluates the major portion of the enzyme.

[Interaction of phospholipids with 3-oxosteroid-delta 1-dehydrogenase in adsorptional model biomembranes. Interaction of the enzyme from Mycobacterium rubrum with liposomes].

A comparative study of the activity of 3-oxosteroid-delta 1-dehydrogenase from Mycobacterium rubrum 121 in solution and after interaction with liposomes prepared from phospholipids of the same microorganism was carried out. It was demonstrated that at pH 6.6 the enzyme activity in the presence of liposomes is increased.

[Mycobacterium rubrum phospholipids].

Mycobacterium rubrum 121 cells contain 8% of lipids, one third of which is represented by phospholipids: cardiolipin, phosphatidyl ethanolamine, phosphatidyl inositol and phosphatidyl inositolmannosides. The acyl groups of these phospholipids are residues of C14-C19 fatty acids, with palmitic and oleic acids prevailing. Differences were found in the fatty acid composition of certain phospholipids.

[3-oxosteroid-delta 1-dehydrogenase localization in Mycobacterium rubrum and Arthobacter globiformis cells].

Osmotically susceptible forms were obtained from Mycobacterium rubrum and Arthrobacter globiformis (Mycobacterium globiforme) cells. The activity of 3-oxosteroid-delta 1-dehydrogenase was comparatively estimated in subcellular fractions after differential centrifugation of cell homogenates prepared either mechanically or by lysis of osmotically susceptible forms. The results indicate that the enzyme is located in the cells of the above microorganisms in both the free state (in the fraction of soluble proteins) and the membrane-bound form.