Linked Life Data

3967486

Source:http://linkedlifedata.com/resource/pubmed/id/3967486

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1985-3-21
pubmed:abstractText
NADH-cytochrome b5 reductase from hog gastric microsomes was studied with respect to substrate dependence, optimum pH, thermal denaturation as well as anti-cytochrome b5 antibodies and different ions. The reduction of potassium ferricyanide by the enzyme was specific for NADH. Using potassium ferricyanide or trypsin-solubilized liver cytochrome b5 (Tb5) as substrates, enzyme activity was inhibited by ADP and to a lesser extent by ATP. Tb5- (but not ferricyanide-) reductase was activated by ionic strength up to 0.05 ion equivalent per liter and inhibited at higher strengths whatever the ion used (Cl-, Na+, Ca2+, Mg2+). Enzyme solubilization occurred with Triton X100. The solubilization increased the Tb5- (but not the ferricyanide-) reductase activity up to a Triton:protein ratio of 15. We therefore suggest that gastric microsomes contain a Triton soluble membrane-bound NADH cytochrome b5 reductase which is in many respects similar to the liver and red cell enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0305-0491
pubmed:author
pubmed:issnType
Print
pubmed:volume
80
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Gastric microsomal NADH-cytochrome b5 reductase: characterization and solubilization.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't