Linked Life Data

6808494

Source:http://linkedlifedata.com/resource/pubmed/id/6808494

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-9-10
pubmed:abstractText
Several methods for the isolation of apparently homogeneous pig kidney diamine oxidase have been reported in recent years (1-7), but these procedures allow to obtain only little amounts of material making very difficult the study of the molecular properties of the enzyme. Drawing useful indication from the purification procedures previously reported, we were able to set up a new method which allows to obtain homogeneous enzyme samples in high yield and with good reproducibility. This procedure allowed to determine with greater accuracy the molecular weight of the enzyme that resulted to be 170,000 daltons by gel chromatography and 145,000 by ultracentrifuge. The enzyme is composed of two apparently identical subunits and contains two copper atoms per dimer. The amino acid composition of the protein has been also worked out and found similar to those already reported for other copper dependent amine oxidases. Pig kidney diamine oxidase is a glycoprotein containing about 20% sugars by weight.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0032-7484
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-28
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Diamine oxidase from pig kidney: new purification method and amino acid composition.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't