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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1997-3-28
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pubmed:databankReference | |
pubmed:abstractText |
Between days 11 and 12 of gestation, the porcine conceptus undergoes a metamorphosis from a spherical blastocyst to an elongate thread-like form. During this process, the conceptus secretes a variety of products. One of these products is protein previously referred to as porcine embryonic basic protein (BP). This protein has been shown to be a major secreted product between days 13 and 18. In this study, we report a simple two-step procedure to isolate BP from day 15 porcine conceptus conditioned medium, utilized ion-exchange chromatography and reverse-phase HPLC. Purified BP was subjected to Edman degradation amino-terminal sequencing and a 25 amino acid residue sequence was obtained. Comparing the N-terminal sequence of BP to sequences in the GenBank database determined that BP shared amino acid homology with porcine pregnancy-associated glycoprotein-2 (PAG-2). The region of identity corresponded to an internal site of PAG-2, suggesting BP was a proteolytic fragment of PAG-2. The purified protein was confirmed to be BP by Western blot using a previously characterized anti-BP antiserum. Also, the BP was immunolocalized with the trophectoderm of day 11 blastocysts. Staining intensity was diminished in spherical blastocysts compared to elongated blastocysts. Although the function of PAG-2 and its cleavage product BP are unknown, the large quantity produced by the porcine conceptus and its sequence conservation across species may indicate a necessary role in early pregnancy.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Conditioned,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Pregnancy Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/pregnancy-associated glycoprotein 1,
http://linkedlifedata.com/resource/pubmed/chemical/pregnancy-associated glycoprotein 2
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1357-2725
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1249-55
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9022284-Amino Acid Sequence,
pubmed-meshheading:9022284-Animals,
pubmed-meshheading:9022284-Aspartic Acid Endopeptidases,
pubmed-meshheading:9022284-Blastocyst,
pubmed-meshheading:9022284-Culture Media, Conditioned,
pubmed-meshheading:9022284-Female,
pubmed-meshheading:9022284-Gestational Age,
pubmed-meshheading:9022284-Immunohistochemistry,
pubmed-meshheading:9022284-Molecular Sequence Data,
pubmed-meshheading:9022284-Peptide Fragments,
pubmed-meshheading:9022284-Pregnancy,
pubmed-meshheading:9022284-Pregnancy Proteins,
pubmed-meshheading:9022284-Sequence Homology, Amino Acid,
pubmed-meshheading:9022284-Swine
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pubmed:year |
1996
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pubmed:articleTitle |
Isolation and identification of porcine embryonic basic protein as a fragment of pregnancy-associated glycoprotein-2.
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pubmed:affiliation |
Department of Animal Science, University of Tennessee, Knoxville 37901, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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