title: Some kinetic and molecular properties of yeast phosphofructokinase.
abstract: Yeast PFK had a sedimentation coefficient of 16.7 S both in the absence and in the presence of ATP, and did not dissociate even at very low protein concentrations. Sodium dodecyl-sulphate caused dissociation of the protein to sub-units of 3.2 S.The effects of pH on substrate affinities are described. In the presence of UTP, acting as non-inhibiting phosphate donor, the behaviour of the enzyme towards F-6-P was co-operative, with a Hill coefficient of 2.2.
authors.affiliation: Institute of Physiological Chemistry, Karl-Marx-University, Leipzig, Germany
authors.forename: G
authors.initials: G
authors.lastname: Kopperschläger
authors.forename: R
authors.initials: R
authors.lastname: Freyer
authors.forename: W
authors.initials: W
authors.lastname: Diezel
authors.forename: E
authors.initials: E
authors.lastname: Hofmann