Linked Life Data

6407957

Source:http://linkedlifedata.com/resource/pubmed/id/6407957

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1983-8-11
pubmed:abstractText
Human liver apolipoprotein AI and A II poly(A+) mRNA has been translated in the cell-free rabbit reticulocyte lysate system. The structures of the two primary translation products of these two main protein components of human serum high-density lipoprotein (HDL) have been characterized. The products of the synthesis in vitro are preproapolipoproteins. The signal sequence (pre-sequence) of the primary translation product of human apo AI mRNA consists of 18 amino acids, that of apo AII of 17 amino acids. The cotranslational translocation into dog microsomal vesicles is associated with the cleavage of these sequences by the signal peptidase releasing the proapolipoproteins AI and AII, both extended by an N-terminal hexapeptide. Preproapolipoprotein AII is synthesized in its monomeric form consisting of 100 amino acids. Pro-apo AII is present in the vesicles of the endoplasmic reticulum also as monomer. Sequencing of the radiolabelled signal sequences of both pre-forms revealed their strongly hydrophobic nature. Despite the high affinity of HDL-apolipoproteins for complex lipids their secretion requires these hydrophobic signal sequences for translocation. Internal recognition sequences in the native apoproteins are not responsible for the transmembrane transport.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0018-4888
pubmed:author
pubmed:issnType
Print
pubmed:volume
364
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
227-37
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Cell-free translation of human liver apolipoprotein AI and AII mRNA. Processing of primary translation products.
pubmed:publicationType
Journal Article