Linked Life Data

6342999

Source:http://linkedlifedata.com/resource/pubmed/id/6342999

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1983-7-15
pubmed:abstractText
The sucrase-isomaltase complex (SI) of the small intestinal brush border membrane accounts for approximately 9-10% of the intrinsic protein. The isomaltase subunit alone interacts with the membrane directly, via a highly hydrophobic segment at its N-terminal region. This segment has a helical conformation for more than 85% and crosses the membrane twice, the N-terminus being located at the outer, luminal side of the membrane. The sucrase subunit is attached to the membrane solely via its interactions with the isomaltase subunit. The sucrase-isomaltase complex is synthesized as a single, very long (Mr approximately 260 000) polypeptide chain (pro-SI, carrying the two sites of sucrase and isomaltase in an already enzymically active form), with the isomaltase portion corresponding to the N-terminal part of pro-SI. Pro-SI is processed into 'final' SI by pancreatic proteases. Recently the cell-free translation of pro-SI has been achieved in vitro. From a detailed knowledge of the anchoring of SI (and pro-SI) in the membrane it has been possible to suggest one particular mechanism as the most likely for the synthesis, insertion and assembly of pro-SI.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-5208
pubmed:author
pubmed:issnType
Print
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
92-112
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Biosynthesis and assembly of the largest and major intrinsic polypeptide of the small intestinal brush borders.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't