Primary structure, physicochemical properties, and chemical modification of NAD(+)-dependent D-lactate dehydrogenase. Evidence for the presence of Arg-235, His-303, Tyr-101, and Trp-19 at or near the active site.-Reference-Cited by-同舟云学术

Primary structure, physicochemical properties, and chemical modification of NAD(+)-dependent D-lactate dehydrogenase. Evidence for the presence of Arg-235, His-303, Tyr-101, and Trp-19 at or near the active site.

Published:1992-04 Issue:12 Volume:267 Page:8499-8513
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Kochhar S,Hunziker P.E.,Leong-Morgenthaler P,Hottinger H

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference71 articles.

1. Refined crystal structure of dogfish M4 apo-lactate dehydrogenase

2. Zuordnung eines essentiellen Histidinrestes der Lactat-Dehydrogenase zur Substratbindungsstelle

3. The presence of a histidine-aspartic acid pair in the active site of 2-hydroxyacid dehydrogenases. X-ray refinement of cytoplasmic malate dehydrogenase.

4. Affinity chromatography of phosphofructokinase using Cibacron blue F3G-A

5. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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