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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
25
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pubmed:dateCreated |
1988-5-3
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pubmed:databankReference | |
pubmed:abstractText |
The primary structure of human placental anticoagulant protein was determined by a combination of amino acid and nucleotide sequencing techniques. The carboxymethylated protein was digested with cyanogen bromide, and the resulting peptides were separated by gel filtration and high-performance liquid chromatography. A total of 239 out of 319 amino acid residues were identified from 7 cyanogen bromide fragments. A full-length cDNA clone encoding placental anticoagulant protein was isolated from a human placenta cDNA library. This clone was 1.6 kilobases long and contained a translation initiation site coding for methionine, 957 nucleotides encoding for the mature protein, a stop codon, a poly(A) recognition site, and a poly(A) tail. Analysis of the tryptic-blocked peptide that originated from the NH2-terminus of the protein showed that the terminal methionine was removed and the adjacent alanine residue was acetylated by posttranslational events. Placental anticoagulant protein is composed of 319 amino acids with acetylalanine as the NH2-terminus and has a high degree of sequence identity with lipocortins I and II. It contains four internal repeats, each including a sequence corresponding to a putative Ca2+-dependent phospholipid binding site. Placental anticoagulant protein is a member of the lipocortin/calpactin family.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Annexins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyanogen Bromide,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Pregnancy Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8087-92
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2964863-Amino Acid Sequence,
pubmed-meshheading:2964863-Annexins,
pubmed-meshheading:2964863-Base Sequence,
pubmed-meshheading:2964863-Cyanogen Bromide,
pubmed-meshheading:2964863-DNA,
pubmed-meshheading:2964863-Female,
pubmed-meshheading:2964863-Genes,
pubmed-meshheading:2964863-Glycoproteins,
pubmed-meshheading:2964863-Humans,
pubmed-meshheading:2964863-Molecular Sequence Data,
pubmed-meshheading:2964863-Peptide Fragments,
pubmed-meshheading:2964863-Placenta,
pubmed-meshheading:2964863-Pregnancy Proteins,
pubmed-meshheading:2964863-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:2964863-Sequence Homology, Nucleic Acid
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pubmed:year |
1987
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pubmed:articleTitle |
Primary structure of human placental anticoagulant protein.
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pubmed:affiliation |
Department of Biochemistry, University of Washington, Seattle 98195.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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