Linked Life Data

2282062

Source:http://linkedlifedata.com/resource/pubmed/id/2282062

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1991-3-12
pubmed:abstractText
Glucose-6-phosphate dehydrogenase (EC 1.1.1.49) has been purified from methanol grown Pseudomonas W6 by a simple procedure involving dye-ligand affinity chromatography on Cibacronblue F3G-A-Sephadex and Procion Red HE-3B-Sepharose. The purification procedure yielded a homogeneous enzyme with (1) high specific activity of 390 and 500 units/mg with NADP and NAD, respectively, and (2) low concentrations of contaminating activities. The molecular mass of the native enzyme was estimated to be 123 +/- 5 kDa. For the polypeptide chain after SDS denaturation a molecular mass of about 61 kDa was calculated. The kinetic behaviour of glucose-6-phosphate dehydrogenase exhibiting activity with either NADP or NAD was studied with respect to the substrate and coenzyme affinities and to ATP inhibition of enzyme activity. The applicability of prepared glucose-6-phosphate dehydrogenase as an auxiliary enzyme in clinical tests is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0232-766X
pubmed:author
pubmed:issnType
Print
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
539-46
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Purification and characterization of glucose-6-phosphate dehydrogenase from Pseudomonas W6.
pubmed:affiliation
Institute of Biochemistry, Karl Marx University, Leipzig, GDR.
pubmed:publicationType
Journal Article