Linked Life Data

10920432

Source:http://linkedlifedata.com/resource/pubmed/id/10920432

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2000-10-5
pubmed:abstractText
A constitutive alkaline phosphatase was purified to apparent homogeneity as determined by polyacrylamide gel electrophoresis from mycelia of the wild strain 74A of the mold Neurospora crassa, after growth on acetate and in the presence of saturating amounts of inorganic phosphate (Pi) for 72 h at 30 degrees C. The molecular mass was 58 kDa and 56 kDa as determined by exclusion chromatography and SDS-PAGE, respectively. This monomeric enzyme shows an apparent optimum pH ranging from 9.5 to 10.5 and Michaelis kinetics for the hydrolysis of p-nitrophenyl phosphate (the K(m) and Hill coefficient values were 0.35 mM and 1.01, respectively), alpha-naphthyl phosphate (the K(m) and Hill coefficient values were 0.44 mM and 0.97, respectively), beta-glycerol phosphate (the K(m) and Hill coefficient values were 2.46 mM and 1.01, respectively) and L-histidinol phosphate (the K(m) and Hill coefficient values were 0.47 mM and 0.94, respectively) at pH 8.9. The purified enzyme is activated by Mg(2+), Zn(2+) and Tris-HCl buffer, and is inhibited by Be(2+), histidine and EDTA. Also, 0.3 M Tris-HCl buffer protected the purified enzyme against heat inactivation at 70 degrees C (half-life of 19.0 min, k = 0.036 min(-1)) as compared to 0.3 M CHES (half-life of 2.3 min, k = 0.392 min(-1)) in the same experiment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0100-879X
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
905-12
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Properties of a constitutive alkaline phosphatase from strain 74A of the mold Neurospora crassa.
pubmed:affiliation
Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brasil.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't