[Ribonuclease Ap1 from Aspergillus pallidus. Purification, primary structure and crystallization].

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.

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].

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.