Linked Life Data

7905327

Source:http://linkedlifedata.com/resource/pubmed/id/7905327

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1994-3-8
pubmed:abstractText
D-amino acid oxidase from Trigonopsis variabilis was purified to homogeneity as a well resolved flavoprotein. Specific activity of pure enzyme was 86.6 U/mg at 30 degrees C and pH 8.5. Optimum pH for enzyme activity was 7.5 and optimum temperature was 55 degrees C. The enzyme is a non-glycosylated homodimer; the protein monomer had a M(r) of 38 +/- 2 kDa and contained one molecule of non covalently bound FAD per mole of monomer. A single molecular form with an isoelectric point of 5.1 was detected in isoelectrofocusing. The A272/A455 ratio as calculated from the absorbance spectrum was 8.4. The enzyme bound competitive inhibitors benzoate and anthranilate giving typical flavin spectral perturbations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
709-17
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Characterization of D-amino acid oxidase from Trigonopsis variabilis.
pubmed:affiliation
Department of General Physiology and Biochemistry, University of Milano, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't