Linked Life Data

11934582

Source:http://linkedlifedata.com/resource/pubmed/id/11934582

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2002-4-5
pubmed:abstractText
Di-/tri- and especially tetrapeptides incorporating the sequence DADD present in the carboxyterminal region of the bicarbonate/chloride anion exchanger AE1 strongly activate human carbonic anhydrase (CA) isozyme II, whereas they act as more inefficient activators of isozymes I and IV. This discovery suggests that in the metabolon hCA II-AE1, the last protein plays a role both as a CA activator as well as a bicarbonate transporter. A synthesis of the tripeptide DAD and the tetrapeptide DADD is also presented together with the possible explanation why such highly acidic oligopeptides efficiently bind to hCA II but not to the closely related isozymes I and IV.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0960-894X
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1177-80
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Carbonic anhydrase activators: human isozyme II is strongly activated by oligopeptides incorporating the carboxyterminal sequence of the bicarbonate anion exchanger AE1.
pubmed:affiliation
Università degli Studi di Firenze, Dipartimento di Chimica, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia, 3, I-50019, Sesto Fiorentino (Firenze), Italy.
pubmed:publicationType
Journal Article