Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1997-3-28
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1357-2725
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1249-55
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Isolation and identification of porcine embryonic basic protein as a fragment of pregnancy-associated glycoprotein-2.
pubmed:affiliation
Department of Animal Science, University of Tennessee, Knoxville 37901, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't