title: [Purification and properties of glucoamylase from Endomycopsis sp. 20-9].
abstract: Homogenous yeast (Endomycopsis sp. 20-9) glucoamylase was isolated from cultural medium. The homogeneity of the enzyme preparation is demonstrated by means of polyacrylamide gel disc electrophoresis, isofocusing and ultracentrifugation. Amino acid composition, molecular weight (53 000), sedimentation constant (4.3S) and isoelectric point (pI 3.80-3.82) of the enzyme are determined. Glucoamylase is found to be glucoprotein.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001203:Ascomycota / Q000201:enzymology*; D055598:Chemical Phenomena; D002621:Chemistry; D005087:Glucan 1,4-alpha-Glucosidase / Q000302:isolation & purification*; D005959:Glucosidases / Q000302:isolation & purification*; D006023:Glycoproteins / Q000032:analysis; D007526:Isoelectric Point; D008970:Molecular Weight; D004718:Saccharomycetales / Q000201:enzymology*
chemical_list: D000596:Amino Acids; D006023:Glycoproteins; D005959:Glucosidases; D005087:Glucan 1,4-alpha-Glucosidase
vernacular_title: Ochistka i svoĭstva gliukoamilazy Endomycopsis sp. 20-9.