Linked Life Data

6773961

Source:http://linkedlifedata.com/resource/pubmed/id/6773961

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1980-11-24
pubmed:abstractText
the sequence of the low activity form of equine erythrocyte carbonic anhydrase has been determined. The most common electrophoretic form, designated D, has been found to have five substitutions. Amino acid exchanges in the electrophoretic variants known as A1, A2, B, and T have been found at six other positions. The data do not permit calculation of the number of polymorphic forms of this enzyme. The equine D isozyme and the analogous human enzyme are quite homologous, 211 of their 260 residues, or 81%, being identical.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
255
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9196-204
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Sequence of the low activity equine erythrocyte carbonic anhydrase and delineation of the amino acid substitutions in various polymorphic forms.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.