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half cystine/horenso
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Purification and comparative characterization of an enolase from spinach.
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An enolase has been purified to apparent homogeneity, as measured by gel electrophoresis, some 400-fold from spinach (Spinacia oleracea). This is the first plant enolase that has been purified to homogeneity. At moderate ionic strengths, the 5,5-dithio-bis-2-(nitrobenzoate) (DTNB)-or
Carbonic anhydrase from spinach leaves. Isolation and some chemical properties.
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Spinach carbonic anhydrase has been purified by modification and extension of a published method (Pocker, Y., and Ng. J. S. U. (1973) Biochemistry 12, 5127-5134), using (NH4)2SO4 precipitation and chromatography on DEAE-cellulose, agarose, and DEAE-Sephadex. The enzyme so obtained was homogeneous by
Properties of a thioredoxin purified from rabbit bone marrow which fails to serve as a hydrogen donor for the homologous ribonucleotide reductase.
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A thioredoxin has been highly purified from rabbit bone marrow. This thioredoxin is heat-stable, has a molecular weight of approximately 13,000, and contains 4 half-cystines. It is a substrate for the NADPH-dependent thioredoxin reductase of rabbit bone marrow, catalyzes the reduction of insulin
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