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Literature DB >> 3800969

Purification and subunit structure of phosphoglycerate dehydrogenase from rabbit liver.

Abstract

D-3-Phosphoglycerate dehydrogenase (EC 1.1.1.95) was purified from rabbit liver by (NH4)2SO4 fractionation, DEAE-Sephacel chromatography, affinity chromatography on AMP-agarose and molecular-sieve h.p.l.c. The purified enzyme was homogeneous as judged by SDS/polyacrylamide-slab-gel electrophoresis. On the basis of molecular-sieve h.p.l.c. and SDS/polyacrylamide-gel electrophoresis, the enzyme is a tetramer composed of subunits of Mr 60,000.

Entities: Chemical Species

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Year: 1986 PMID： 3800969 PMCID： PMC1147222 DOI： 10.1042/bj2380919

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

16 in total

1. D-3-phosphoglycerate dehydrogenase from hog spinal cord-1.

Authors: R D Field; H J Sallach
Journal: Methods Enzymol Date: 1975 Impact factor: 1.600

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

Authors: M M Bradford
Journal: Anal Biochem Date: 1976-05-07 Impact factor: 3.365

3. N6-immobilized 5 -AMP and NAD+: preparations and applications.

Authors: M J Harvey; D B Craven; C R Lowe; P D Dean
Journal: Methods Enzymol Date: 1974 Impact factor: 1.600

4. AMP and NAD as "General Ligands".

Authors: K Mosbach
Journal: Methods Enzymol Date: 1974 Impact factor: 1.600

5. The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase.

Authors: E Sugimoto; L I Pizer
Journal: J Biol Chem Date: 1968-05-10 Impact factor: 5.157

Purification and subunit structure of phosphoglycerate dehydrogenase from rabbit liver.

1. D-3-phosphoglycerate dehydrogenase from hog spinal cord-1.

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

3. N6-immobilized 5 -AMP and NAD+: preparations and applications.

4. AMP and NAD as "General Ligands".

5. The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase.

6. Subcellular fractionation of rat liver.

7. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

8. Transient kinetic and deuterium isotope effect studies on the catalytic mechanism of phosphoglycerate dehydrogenase.

9. Transient kinetic studies on the allosteric transition of phosphoglycerate dehydrogenase.

10. D-3-Phosphoglycerate dehydrogenase from chicken liver. I. Purification.

1. Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase.

2. An epitope tag alters phosphoglycerate dehydrogenase structure and impairs ability to support cell proliferation.