Ornithine cyclase (deaminating). II. Properties of the homogeneous enzyme.

摘要: Abstract Ornithine cyclase from Clostridium sporogenes was purified to electrophoretic and ultracentrifugal homogeneity. The pure had a sedimentation coefficient (s20,w) of 5.6 S measured by high speed velocity centrifugation, molecular weight 81,000 calculated equilibrium sedimentation. Amino acid analysis indicated 80,000 partial specific volume 0.733 cm3 per g for the protein. Gel electrophoresis on polyacrylamide in presence sodium dodecyl sulfate enzyme made up two subunits equal size each with 41,500. light absorption spectrum major peak at 277 nm, calculations based absorbance values 280 260 nm approximately 1 mol pyridine nucleotide cyclase. Assay bound NAD+ demonstrated enzyme. activity stimulated either ADP or ATP. Chromatography DEAE-cellulose columns dramatically increased dependence added NAD+. It inhibited severely oxygen several sulfhydryl group inhibitors.