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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.

A novel hydroxypyruvate reductase preferring NADPH to NADH as a cofactor was purified over 1500-fold from spinach leaf extracts. The enzyme was an oligomer of about 70 kDa, composed of two subunits of 38 kDa each. The Km for hydroxypyruvate (with NADPH) was about 0.8 mM in the pH range 5.5-6.5, and...

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Detaylı Bibliyografya
Asıl Yazarlar: Kleczkowski, L A, Randall, D D
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1988
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC1148826/
https://ncbi.nlm.nih.gov/pubmed/3281657
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