[Ribonuclease Ap1 from Aspergillus pallidus. Purification, primary structure and crystallization]. / Ribonukleaza Ap1 Aspergillus pallidus. Ochistka, opredelenie pervichnoi struktury i kristallizatsiia.

Extracellular guanyl-specific RNAase of the fungus Aspergillus pallidus (RNAase ApI) was isolated in preparative amounts with a 40% yield and purified to homogeneity (938-fold). The complete amino acid sequence of the protein (104 amino acid residues) was determined: 6 Asp, 4 Asn, 4 Thr, 14 Ser, 3 Glu, 4 Gln, 4 Pro, 15 Gly, 9 Ala, 4 Cys, 6 Val, 2 Ile, 4 Leu, 10 Tyr, 4 Phe, 3 His, 4 Arg, 1 Trp. RNAase ApI has a molecular mass of 11,029 Da and is homologous to the family of fungal extracellular guanyl-specific RNAases. The primary structure of the protein is close to that of RNAase C2 from Asp. clavatus and differs from it by only 4 substitutions of amino acid residues. Monocrystals of RNAase ApI were grown which can be used for the X-ray analysis of proteins.

Determination of localization of ribonuclease in Aspergillus clavatus.

Indirect fluorescent antibody method was used to demonstrate the localization of A. clavatus ribonuclease in apical cell ends. Using protoplasts, ribonuclease was found to be present mainly in the periplasmic space.

[Several properties of beta-galactosidase from Artemisia annua L]. / Nekotorye svoistva beta-galaktozidazy iz Artemisia annua L.

beta-Galactosidase was isolated from different organs of the wormwood (Artemisia annua L.). The enzyme activity was found to change during the growth and development of the plant. The maximal activity was revealed in reproductive organs at flowering and fruiting stages. Using ion-exchange chromatography, isoelectric focusing and disc electrophoresis in PAAG, two molecular isoforms of beta-galactosidase were detected. Some physicochemical properties of the enzyme were investigated.