title: [Investigation of permolecular structure of lipase from Rhizopus niveus].
abstract: It has been shown by classical biophysical and biochemical methods in combination with atomic microscopy that lipase from Rhizopus niveus exists in a water solution as a dimer with a molecular weight of 96 kDa. The rate of splitting of triglycerides by a dimeric molecules is twice that of monomers. The heat stability of the monomeric form of lipase at temperatures of 20-60 degrees C is significantly higher than that of the native molecule.
authors.forename: T A
authors.initials: TA
authors.lastname: Kovaleva
authors.forename: A S
authors.initials: AS
authors.lastname: Belenova
authors.forename: L A
authors.initials: LA
authors.lastname: Bitiutskaia
authors.forename: O D
authors.initials: OD
authors.lastname: Trofimova
authors.forename: M V
authors.initials: MV
authors.lastname: Grechkina
authors.forename: O P
authors.initials: OP
authors.lastname: Bagno
authors.forename: V G
authors.initials: VG
authors.lastname: Artiukhov
mesh_terms: D005656:Fungal Proteins / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D012233:Rhizopus / Q000201:enzymology*; D014280:Triglycerides / Q000737:chemistry*
chemical_list: D005656:Fungal Proteins; D014280:Triglycerides; D008049:Lipase