Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-9-22
pubmed:abstractText
Glucokinase from dog liver has been purified to homogeneity by a procedure involving DEAE-cellulose chromatography, ammonium sulfate fractionation, gel filtration chromatography, and affinity chromatography on glucosamine-Sepharose. The purified enzyme was characterized with respect to stability, molecular weight, amino acid composition, SH groups, and physicochemical and kinetic properties. A molecular weight of 49,000 and 47,000 was estimated by sodium dodecylsulfate gel electrophoresis and gel filtration in non-denaturing conditions, respectively, indicating a monomeric structure for the enzyme. Glucokinase exhibits a sigmoidal saturation function for glucose with a Hill coefficient of 1.5 and a half-saturation value of 4mM at pH 7.5.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0004-0533
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
271-86
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Purification and characterization of dog liver glucokinase.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't