(Q24529510)

English

Purification and characterization of a novel NADPH(NADH)-dependent hydroxypyruvate reductase from spinach leaves. Comparison of immunological properties of leaf hydroxypyruvate reductases

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scholarly article

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Purification and characterization of a novel NADPH(NADH)-dependent hydroxypyruvate reductase from spinach leaves. Comparison of immunological properties of leaf hydroxypyruvate reductases (English)

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1 reference

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author name string

L A Kleczkowski

1

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D D Randall

2

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language of work or name

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publication date

15 February 1988

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Biochemical Journal

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250

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1

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145-52

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Inhibition of Spinach Leaf NADPH(NADH)-Glyoxylate Reductase by Acetohydroxamate, Aminooxyacetate, and Glycidate

1 reference

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24 March 2017

Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase

1 reference

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Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Localization and properties of hydroxypyruvate and glyoxylate reductases in spinach leaf particles

1 reference

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Properties of a new glyoxylate reductase from leaves

1 reference

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30 May 2018

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1 reference

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Metabolism of glycolate and glyoxylate in intact spinach leaf peroxisomes.

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29 November 2018

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Serine: glyoxylate, alanine:glyoxylate, and glutamate:glyoxylate aminotransferase reactions in peroxisomes from spinach leaves

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Peroxisomal localization and properties of tryptophan aminotransferase in plant leaves

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Provisions of reductant for the hydroxypyruvate to glycerate conversion in leaf peroxisomes : a critical evaluation of the proposed malate/aspartate shuttle

1 reference

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Conversion of serine to glycerate in intact spinach leaf peroxisomes: role of malate dehydrogenase

1 reference

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12 December 2020

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The Structural Properties of Spinach Leaf Glyoxylic Acid Reductase

1 reference

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12 December 2020

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Identifiers

10.1042/BJ2500145

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