Purification, characterization, and immunocytochemical localization of the major basic protein of pig blastocysts
The major basic protein (BP) synthesized and secreted by elongating pig blastocysts was purified from medium of Day 14-17 conceptus cultures. Sequential ion-exchange and gel-filtration chromatographies resulted in isolation of BP as a single polypeptide of Mr = 43,100 or 42,800 under denaturing or n...
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| Veröffentlicht in: | Biology of reproduction 1988-12, Vol.39 (5), p.1171-1182 |
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| creator | Baumbach, G.A Climer, A.H Bartley, N.G Kattesh, H.G Godkin, J.D |
| description | The major basic protein (BP) synthesized and secreted by elongating pig blastocysts was purified from medium of Day 14-17
conceptus cultures. Sequential ion-exchange and gel-filtration chromatographies resulted in isolation of BP as a single polypeptide
of Mr = 43,100 or 42,800 under denaturing or native conditions, respectively. BP was found to be a glycoprotein by incorporation
of [3H] glucosamine and susceptibility to N-glycopeptidase F. Two BP polypeptides were produced by N-glycopeptidase F (Mr
= 39,800 and 36,300). Antiserum to BP immunoprecipitated radiolabeled BP from blastocyst culture medium. BP was not detected
in medium from 1-2 mm diameter spherical (Day 10) blastocysts but was found in medium from 3-5 mm spherical (Day 10) and filamentous
(less than 50 cm, Day 12) conceptuses, suggesting that BP synthesis and secretion began at the initiation of trophoblast expansion.
With immunocytochemical procedures, BP was located in the apical cytoplasm of trophectoderm cells of Day 11 expanding (5-7
and 10-20 mm) blastocysts. These results suggest that trophoblast epithelium secrete BP apically toward the uterine lumen
and that BP may play a role in maternal-fetal interactions during the peri-implantation period. |
| doi_str_mv | 10.1095/biolreprod39.5.1171 |
| format | Article |
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conceptus cultures. Sequential ion-exchange and gel-filtration chromatographies resulted in isolation of BP as a single polypeptide
of Mr = 43,100 or 42,800 under denaturing or native conditions, respectively. BP was found to be a glycoprotein by incorporation
of [3H] glucosamine and susceptibility to N-glycopeptidase F. Two BP polypeptides were produced by N-glycopeptidase F (Mr
= 39,800 and 36,300). Antiserum to BP immunoprecipitated radiolabeled BP from blastocyst culture medium. BP was not detected
in medium from 1-2 mm diameter spherical (Day 10) blastocysts but was found in medium from 3-5 mm spherical (Day 10) and filamentous
(less than 50 cm, Day 12) conceptuses, suggesting that BP synthesis and secretion began at the initiation of trophoblast expansion.
With immunocytochemical procedures, BP was located in the apical cytoplasm of trophectoderm cells of Day 11 expanding (5-7
and 10-20 mm) blastocysts. These results suggest that trophoblast epithelium secrete BP apically toward the uterine lumen
and that BP may play a role in maternal-fetal interactions during the peri-implantation period.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod39.5.1171</identifier><identifier>PMID: 3219388</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>Animals ; basic protein ; Biological and medical sciences ; Blastocyst - metabolism ; blastocytes ; Blood Proteins - analysis ; Blood Proteins - biosynthesis ; Blood Proteins - immunology ; Blood Proteins - isolation & purification ; CELL CULTURE ; Cells, Cultured ; CERDO ; CONCEPTUS ; CULTIVO DE CELULAS ; CULTURE DE CELLULES ; DESARROLLO EMBRIONARIO ; DEVELOPPEMENT EMBRYONNAIRE ; Early stages. Segmentation. Gastrulation. Neurulation ; Embryology: invertebrates and vertebrates. Teratology ; EMBRYONIC DEVELOPMENT ; Eosinophil Granule Proteins ; Female ; Fundamental and applied biological sciences. Psychology ; PEPTIDE ; Peptide Biosynthesis ; PEPTIDES ; Peptides - analysis ; Peptides - immunology ; Peptides - isolation & purification ; PEPTIDOS ; pigs ; PORCIN ; PROTEINAS ; PROTEINE ; PROTEINS ; Ribonucleases ; SECRECION ; SECRETION ; SWINE ; Swine - metabolism</subject><ispartof>Biology of reproduction, 1988-12, Vol.39 (5), p.1171-1182</ispartof><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6821912$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3219388$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Baumbach, G.A</creatorcontrib><creatorcontrib>Climer, A.H</creatorcontrib><creatorcontrib>Bartley, N.G</creatorcontrib><creatorcontrib>Kattesh, H.G</creatorcontrib><creatorcontrib>Godkin, J.D</creatorcontrib><title>Purification, characterization, and immunocytochemical localization of the major basic protein of pig blastocysts</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>The major basic protein (BP) synthesized and secreted by elongating pig blastocysts was purified from medium of Day 14-17
conceptus cultures. Sequential ion-exchange and gel-filtration chromatographies resulted in isolation of BP as a single polypeptide
of Mr = 43,100 or 42,800 under denaturing or native conditions, respectively. BP was found to be a glycoprotein by incorporation
of [3H] glucosamine and susceptibility to N-glycopeptidase F. Two BP polypeptides were produced by N-glycopeptidase F (Mr
= 39,800 and 36,300). Antiserum to BP immunoprecipitated radiolabeled BP from blastocyst culture medium. BP was not detected
in medium from 1-2 mm diameter spherical (Day 10) blastocysts but was found in medium from 3-5 mm spherical (Day 10) and filamentous
(less than 50 cm, Day 12) conceptuses, suggesting that BP synthesis and secretion began at the initiation of trophoblast expansion.
With immunocytochemical procedures, BP was located in the apical cytoplasm of trophectoderm cells of Day 11 expanding (5-7
and 10-20 mm) blastocysts. These results suggest that trophoblast epithelium secrete BP apically toward the uterine lumen
and that BP may play a role in maternal-fetal interactions during the peri-implantation period.</description><subject>Animals</subject><subject>basic protein</subject><subject>Biological and medical sciences</subject><subject>Blastocyst - metabolism</subject><subject>blastocytes</subject><subject>Blood Proteins - analysis</subject><subject>Blood Proteins - biosynthesis</subject><subject>Blood Proteins - immunology</subject><subject>Blood Proteins - isolation & purification</subject><subject>CELL CULTURE</subject><subject>Cells, Cultured</subject><subject>CERDO</subject><subject>CONCEPTUS</subject><subject>CULTIVO DE CELULAS</subject><subject>CULTURE DE CELLULES</subject><subject>DESARROLLO EMBRIONARIO</subject><subject>DEVELOPPEMENT EMBRYONNAIRE</subject><subject>Early stages. Segmentation. Gastrulation. Neurulation</subject><subject>Embryology: invertebrates and vertebrates. Teratology</subject><subject>EMBRYONIC DEVELOPMENT</subject><subject>Eosinophil Granule Proteins</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>PEPTIDE</subject><subject>Peptide Biosynthesis</subject><subject>PEPTIDES</subject><subject>Peptides - analysis</subject><subject>Peptides - immunology</subject><subject>Peptides - isolation & purification</subject><subject>PEPTIDOS</subject><subject>pigs</subject><subject>PORCIN</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>Ribonucleases</subject><subject>SECRECION</subject><subject>SECRETION</subject><subject>SWINE</subject><subject>Swine - metabolism</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuLFTEQhYMo43X0DyhCFuLKvubdyVIGXzCgoLMO6TxuZ0h37iTdXK6_3jjTiDs3VVDnq8OhCoBXGO0xUvz9EHMq_liyo2rP9xj3-BHYYU5U1xMhH4MdQkh0lAr6FDyr9RYhzCihF-CCEqyolDtw930tMURrlpjnd9COphi7-BJ_bRMzOxinaZ2zPS_Zjn5qcIIpt7pBMAe4jB5O5jYXOJgaLWypFh_vpWM8wCGZ2rbPdanPwZNgUvUvtn4Jbj59_Hn1pbv-9vnr1YfrLlAslo4rqZy0nklJZG-FM2IYGHNMGI8dt8FL2gtFLGOCcUmw84IPMhiMnOeB0Evw9sG3RblbfV30FKv1KZnZ57XqXgqGpWL_BTHHCPF78PUGrsPknT6WOJly1tsxm_5m001t1wnFzDbWv5hoIRX-J9gYD-MpFq_rZFJqplSfTieqNNd_ftnAlw9gMFmbQ2leNz-kQgL3hP4GFc2dJg</recordid><startdate>19881201</startdate><enddate>19881201</enddate><creator>Baumbach, G.A</creator><creator>Climer, A.H</creator><creator>Bartley, N.G</creator><creator>Kattesh, H.G</creator><creator>Godkin, J.D</creator><general>Society for the Study of Reproduction</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19881201</creationdate><title>Purification, characterization, and immunocytochemical localization of the major basic protein of pig blastocysts</title><author>Baumbach, G.A ; Climer, A.H ; Bartley, N.G ; Kattesh, H.G ; Godkin, J.D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f316t-5989d8ce488287c6da6bb44d46ae1d5cfe837692c44645821de65b8fa10de5f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Animals</topic><topic>basic protein</topic><topic>Biological and medical sciences</topic><topic>Blastocyst - metabolism</topic><topic>blastocytes</topic><topic>Blood Proteins - analysis</topic><topic>Blood Proteins - biosynthesis</topic><topic>Blood Proteins - immunology</topic><topic>Blood Proteins - isolation & purification</topic><topic>CELL CULTURE</topic><topic>Cells, Cultured</topic><topic>CERDO</topic><topic>CONCEPTUS</topic><topic>CULTIVO DE CELULAS</topic><topic>CULTURE DE CELLULES</topic><topic>DESARROLLO EMBRIONARIO</topic><topic>DEVELOPPEMENT EMBRYONNAIRE</topic><topic>Early stages. Segmentation. Gastrulation. Neurulation</topic><topic>Embryology: invertebrates and vertebrates. Teratology</topic><topic>EMBRYONIC DEVELOPMENT</topic><topic>Eosinophil Granule Proteins</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>PEPTIDE</topic><topic>Peptide Biosynthesis</topic><topic>PEPTIDES</topic><topic>Peptides - analysis</topic><topic>Peptides - immunology</topic><topic>Peptides - isolation & purification</topic><topic>PEPTIDOS</topic><topic>pigs</topic><topic>PORCIN</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>Ribonucleases</topic><topic>SECRECION</topic><topic>SECRETION</topic><topic>SWINE</topic><topic>Swine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Baumbach, G.A</creatorcontrib><creatorcontrib>Climer, A.H</creatorcontrib><creatorcontrib>Bartley, N.G</creatorcontrib><creatorcontrib>Kattesh, H.G</creatorcontrib><creatorcontrib>Godkin, J.D</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Baumbach, G.A</au><au>Climer, A.H</au><au>Bartley, N.G</au><au>Kattesh, H.G</au><au>Godkin, J.D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification, characterization, and immunocytochemical localization of the major basic protein of pig blastocysts</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>1988-12-01</date><risdate>1988</risdate><volume>39</volume><issue>5</issue><spage>1171</spage><epage>1182</epage><pages>1171-1182</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>The major basic protein (BP) synthesized and secreted by elongating pig blastocysts was purified from medium of Day 14-17
conceptus cultures. Sequential ion-exchange and gel-filtration chromatographies resulted in isolation of BP as a single polypeptide
of Mr = 43,100 or 42,800 under denaturing or native conditions, respectively. BP was found to be a glycoprotein by incorporation
of [3H] glucosamine and susceptibility to N-glycopeptidase F. Two BP polypeptides were produced by N-glycopeptidase F (Mr
= 39,800 and 36,300). Antiserum to BP immunoprecipitated radiolabeled BP from blastocyst culture medium. BP was not detected
in medium from 1-2 mm diameter spherical (Day 10) blastocysts but was found in medium from 3-5 mm spherical (Day 10) and filamentous
(less than 50 cm, Day 12) conceptuses, suggesting that BP synthesis and secretion began at the initiation of trophoblast expansion.
With immunocytochemical procedures, BP was located in the apical cytoplasm of trophectoderm cells of Day 11 expanding (5-7
and 10-20 mm) blastocysts. These results suggest that trophoblast epithelium secrete BP apically toward the uterine lumen
and that BP may play a role in maternal-fetal interactions during the peri-implantation period.</abstract><cop>Madison, WI</cop><pub>Society for the Study of Reproduction</pub><pmid>3219388</pmid><doi>10.1095/biolreprod39.5.1171</doi><tpages>12</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3363 |
| ispartof | Biology of reproduction, 1988-12, Vol.39 (5), p.1171-1182 |
| issn | 0006-3363 1529-7268 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78641894 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals basic protein Biological and medical sciences Blastocyst - metabolism blastocytes Blood Proteins - analysis Blood Proteins - biosynthesis Blood Proteins - immunology Blood Proteins - isolation & purification CELL CULTURE Cells, Cultured CERDO CONCEPTUS CULTIVO DE CELULAS CULTURE DE CELLULES DESARROLLO EMBRIONARIO DEVELOPPEMENT EMBRYONNAIRE Early stages. Segmentation. Gastrulation. Neurulation Embryology: invertebrates and vertebrates. Teratology EMBRYONIC DEVELOPMENT Eosinophil Granule Proteins Female Fundamental and applied biological sciences. Psychology PEPTIDE Peptide Biosynthesis PEPTIDES Peptides - analysis Peptides - immunology Peptides - isolation & purification PEPTIDOS pigs PORCIN PROTEINAS PROTEINE PROTEINS Ribonucleases SECRECION SECRETION SWINE Swine - metabolism |
| title | Purification, characterization, and immunocytochemical localization of the major basic protein of pig blastocysts |
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