Linked Life Data

3421706

Source:http://linkedlifedata.com/resource/pubmed/id/3421706

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-10-21
pubmed:abstractText
Bovine liver catalase suffered a biphasic inactivation when exposed to NH2Cl. A rapid and irreversible phase of activity loss was followed by a much slower and reversible inactivation. Removal of tightly bound NADPH from the enzyme decreased the extent of the rapid phase; whereas addition of NADPH augmented it. The catalase from Aspergillus niger, which does not contain bound NADPH, was not nearly as sensitive toward NH2Cl as was the liver enzyme and was not sensitized by added NADPH. NADPH is oxidized by NH2Cl, as evidenced by loss of the 340-nm absorption band, but the product of this oxidation was not NADP+. The rapid inactivation of liver catalase by NH2Cl was accompanied by some bleaching of the bands in the visible, while the slow inactivation was coincident with the appearance of a new band at 570 nm. A tentative explanation for these observations is proposed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
279-85
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
NADPH mediates the inactivation of bovine liver catalase by monochloroamine.
pubmed:affiliation
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't