Linked Life Data

33324

Source:http://linkedlifedata.com/resource/pubmed/id/33324

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1979-4-28
pubmed:abstractText
NADP+-dependent cytoplasmic malic enzyme was purified to homogeneity from mouse kidneys by a two-step procedure involving 8-(6-aminohexyl)-amino-2', 5'-ADP-Sepharose affinity chromatography and DEAE-Sephadex ion exchange chromatography. The biochemical properties of the purified enzyme from DBA/2J mice were characterized. These include the determination of molecular weight and amino acid compositions, steady-state kinetics, thermal stability and inactivations by iodoacetate and urea. The native enzyme is a tetramer with a molecular weight of 270,000.Km's for NADP+, L-malate, NADPH and pyruvate were determined to be 3.3 micrometer, 50 micrometer, 10.5 micrometer respectively. Similar to the pigeon liver enzyme, the mouse enzyme exhibits an ordered kinetic mechanism proceeding with the binding of coenzyme first. The enzyme is only weakly inhibited by ATP and other cellular metabolites. A remarkable similarity in amino acid compositions was found between the mouse and rat liver malic enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Cytoplasmic malic enzyme from mouse kidneys.
pubmed:publicationType
Journal Article