Quasi-elastic light scattering studies on pyruvate oxidase

T. Raj, Patricia Russell, W. H. Flygare, Robert B. Gennis

Research output: Contribution to journalArticlepeer-review

Abstract

Quasi-elastic or dynamic light scattering has been used to examine the translational diffusion properties of the enzyme pyruvate oxidase (pyruvate:ferricytochrome b1 oxidoreductase, EC 1.2.2.2.). Controlled proteolysis of the enzyme converts the native form of the enzyme to a protease-activated form which has a specific activity about 20-fold greater than the native oxidase. Light scattering studies indicate no significant change in the size or shape of pyruvate oxidase as a result of this proteolytic activation. In both cases the enzyme may be characterized as a hydrated sphere with a Stokes radius of about 53 Å. The sedimentation velocity-diffusion technique was used to obtain the molecular weight of this tetrameric enzyme, about 252 000 with a value of f{hook}/f{hook}0 of 1.25.

Original languageEnglish (US)
Pages (from-to)42-49
Number of pages8
JournalBBA - Enzymology
Volume481
Issue number1
DOIs
StatePublished - Mar 15 1977

ASJC Scopus subject areas

  • Medicine(all)

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