Home LiteratureArticle Details
PMID: 1203253 Published · ppublish English Journal Article

Crystallization and properties of rat liver malate dehydrogenase (decarboxylating) (NADP).

Biochimica et biophysica acta ·Vol. 410 ·No. 2 ·1975-12-18 ·Pages 237-42

Wada F, Numata N, Eguchi Y, Sakamoto Y

Abstract

Rat liver malate dehydrogenase (decarboxylating) (NADP) ((L-malate: NADP) oxidoreductase (oxaloacetate-decarboxylating), EC 1.1.1.40) was purified and crystallized from medium containing 30 mM Tris-HCl buffer (pH 7.7), 5 mM MgCl2 and 2 mM 2-mercaptoethanol. The enzyme formed rhomboid crystals free from coenzyme, and appeared homogeneous on isoelectric focusing. The crystalline enzyme had an isoelectric point of pH 6.3. Amino acid analysis showed that it contained more acidic amino acids than basic ones.

MeSH Terms
Amino Acids/analysis Animals Crystallization Liver/enzymology Magnesium Malate Dehydrogenase/analysis,isolation & purification Mercaptoethanol Rats
Chemicals
Amino Acids Mercaptoethanol Malate Dehydrogenase Magnesium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Wada F
Numata N
Eguchi Y
Sakamoto Y
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1975-12-18
Pages
237-42
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com