title: [Aspartate kinase activity of Cyanobacteria Anabaena variabilis].
abstract: Aspartate-kinase (ASK) activity of filamentous cyanobacteria A. variabilis and its dependence on physico-chemical factors and substrate concentration in the reaction mixture have been studied. Three isoenzymes ASK-1, ASK-2 and ASK-3 which differ in the values of pH-optima, molecular weight, isoelectric points and effector of retro-inhibition have been isolated by ion-exchange chromatography. High level of inhibition of summary ASK of the cell-free extract can be reached only in a case of simultaneous addition of all amino acids, the final products of this biosynthetic pathway into the incubation mixture.
authors.forename: T G
authors.initials: TG
authors.lastname: Lysenko
authors.forename: N V
authors.initials: NV
authors.lastname: Koltukova
authors.forename: G Kh
authors.initials: GKh
authors.lastname: Kadyrova
authors.forename: O A
authors.initials: OA
authors.lastname: Shainskaia
mesh_terms: D001222:Aspartate Kinase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D000458:Cyanobacteria / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight
chemical_list: D007527:Isoenzymes; D001222:Aspartate Kinase
vernacular_title: Aspartatkinaznaia aktivnost' tsianobakterii Anabaena variabilis.