Linked Life Data

889843

Source:http://linkedlifedata.com/resource/pubmed/id/889843

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1977-10-31
pubmed:abstractText
A procedure has been developed for the purification of human erythrocyte aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.1.3). The process involves a specific substrate elution of the enzyme from phosphocellulose followed by a reverse ammonium sulfate fractionation. The preparation has been shown to be homogeneous by analytical ultracentrifugation, thin-layer electrophoresis, and polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The enzyme exhibits a specific activity of 16 I.U./mg protein, a Km of 7.1-10(-6) M for fructose 1,6-bisphosphate, and a substrate specificity (Fru-1,6-P2/Fru-1-P) of 40. The native protein in a tetramer of 158 000 molecular weight possessing identical or nearly identical subunits, an isoelectric point of 8.9, a diffusion coefficient of 4.68-10(-7) cm2/s, and a molecular radius of 4.56 nm. The study shows the enzyme to be a type A aldolase resembling other muscle forms in chemical and physical properties as well as amino acid composition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
484
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
188-98
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Purification and characterization of aldolase from human erythrocytes.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.