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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3-4
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pubmed:dateCreated |
1984-6-28
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pubmed:abstractText |
The amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II) has been determined. Two different N-termini are noted, the C1 form having an N-acetyl-serine and the C2 form an N-acetyl-threonine. The sequence of the equine enzyme is most homologous to the human CA-II isozyme, with 224 of the 259 residues being identical.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-2928
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
357-67
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6428393-Amino Acid Sequence,
pubmed-meshheading:6428393-Animals,
pubmed-meshheading:6428393-Carbonic Anhydrases,
pubmed-meshheading:6428393-Cattle,
pubmed-meshheading:6428393-Erythrocytes,
pubmed-meshheading:6428393-Horses,
pubmed-meshheading:6428393-Humans,
pubmed-meshheading:6428393-Isoenzymes,
pubmed-meshheading:6428393-Mice,
pubmed-meshheading:6428393-Polymorphism, Genetic,
pubmed-meshheading:6428393-Rabbits,
pubmed-meshheading:6428393-Species Specificity
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pubmed:year |
1984
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pubmed:articleTitle |
Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-Ser/acetyl-Thr) and homologies to similar mammalian isozymes.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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