The dihydroxy acid dehydratase of Neurospora crassa.

نویسندگان

  • K Kiritani
  • S Narise
  • R P Wagner
چکیده

The dihydroxy acid dehydratase of Neurospora crassa was purified lOOto 150-fold by fractionation with protamine sulfate, ammonium sulfate, Sephadex, and DEAE-Sephadex. It was found that the purified protein migrated in an electric field as a single band on acrylamide gel and in the analytical centrifuge. It had a lipid content of 44 to 50%. The enzyme activity was stabilized by the presence of magnesium ion. The Km values and pH optima were determined for both substrates, o(, fl-dihydroxyisovalerate and a!, P-dihydroxy-P-methylvalerate.

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 241 9  شماره 

صفحات  -

تاریخ انتشار 1966