[Interaction of human albumin with sorbents containing immobilized dyes].

Interaction of human albumin with immobilized dye-adsorbents was investigated by frontal chromatographic analysis and static adsorption. The relative strength of the interaction is diminished in the following order: cibacron blue F3GA, orange 4K, claret CT, orange 5K, red-brown 2KT, light resistant yellow 2KT, bright blue KX, scarlet 2Zh, bright red 6C, bright yellow 53, red-brown 2K, golden yellow 2KX, scarlet 4ZhT and yellow 2KT. Following this order the absorbents can be used for purification of human albumin from non-specific impurities taking into account stronger adsorption of albumin or impurities.

[Immobilization of urease from Staphylococcal saprophyticus L-1 on activated silica].

The paper deals with immobilization of urease obtained from Staphylococcus saprophyticus L-1 on the organic silica surfaces. The process completion time (4-5 h) and the optimal pH of binding (7-8) are practically independent of the chemical nature of the carrier surface. The value of the specific activity of urease grafted to silica depends not only on the type of the enzyme-carrier bond, but also on the macromolecule protein-to-silica distance.

[Interaction of NAD(H)-dependent dehydrogenases with active dyes and their complexes with transitional metal ions].

The interaction of NAD(H)-dependent dehydrogenases--yeast alcohol dehydrogenase and rabbit muscle lactate dehydrogenase--with reactive dyes produced in the USSR was studied. The essential role of metal ions in specific binding of alcohol dehydrogenase and dyes was demonstrated by differential spectroscopy, circular dichroism spectroscopy and chromatography. Lactate dehydrogenase in contrast with alcohol dehydrogenase does not require metal ions for the binding of the above-said dyes.

[Properties of the phospholipases C from Bacillus cereus].

Three different phospholipases C--the so-called phospholipase C which hydrolyses phosphatidylcholine (Pch-PLC), sphingomyelinase (SM-PLC) and phosphatidylinositol hydrolysing phospholipase C (PI-PLC)--were separated from the culture filtrate of Bacillus cereus using column chromatography on DEAE-sephadex A-50. The pI values were estimated to be 5.0 +/- 0.

[Purification and properties of alpha-amylases in morphological variants of Bacillus subtilis].

Extracellular alpha-amylases were isolated from the culture medium filtrates of Bacillus subtilis R-623 morphological variants R, P and S by means of biospecific chromatography on artificial sorbents and then purified to homogeneity. Some properties of purified alpha-amylases were being studied. The molecular weight of alpha-amylases from Bacillus subtilis variants R, P and S equals 57,000, 58,000 and 56,000, and the isoelectric points are at pH 5.