Linked Life Data

7244325

Source:http://linkedlifedata.com/resource/pubmed/id/7244325

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1981-8-27
pubmed:abstractText
Arginase (E.C. 3.5.3.1) the enzyme which catalyses the hydrolysis of arginine to ornithine and urea has been investigated in guinea pig liver in relation to the kinetic constants of its substrate and inhibitors as well as to other physico-chemical properties. The results show that the enzyme has Km value of 19.6 mM for its substrate L-arginine and is competitively inhibited by one of its reaction products, the L-ornithine, and also by L-lysine and diaminopymelic acid. Optimal activity of the enzyme occurs at 10.5 pH and maximal stability in the range of 6.5 to 7.5 pH. The mentioned arginase exhibits temperature dependent activity and stability, being 64 degrees C (15 min and pH 7.5) the half-inactivation temperature. An increase in the activity and temperature stability of the enzyme, when previously activated by heating for 5 min at 45 degrees C in the presence of 10 mM MnCl2, has been achieved.
pubmed:language
spa
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0034-9402
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-44
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
[Physico-chemical properties of guinea pig liver arginase (author's transl)].
pubmed:publicationType
Journal Article, English Abstract, Research Support, Non-U.S. Gov't