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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
08/11/2002 |
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Data da última atualização: |
03/10/2016 |
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Autoria: |
GARBAYO, J. M.; REMY, B.; ALABART, J. L.; FOLCH, J.; WATTIEZ, R.; FALMAGNE, P.; BECKERS, J. F. |
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Título: |
Isolation and partial characterization of a pregnancy-associated glycoprotein family from the goat placenta. |
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Ano de publicação: |
1998 |
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Fonte/Imprenta: |
Biology of Reproduction, v. 58, n. 1, p.109-115, 1998. |
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Idioma: |
Inglês |
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Conteúdo: |
Antigen(s) immunologically related to pregnancy-associated glycoproteins (PAGs) have previously been detected in the serum of pregnant goats. In this work, we describe a partial characterization of a family of PAGs isolated from the placenta of the goat. The procedure, monitored by RIA, included extraction of proteins at neutral pH, acidic, and ammonium sulfate precipitations; and gel filtration and ion exchange chromatographies. Immunoreactivity, initially located in the acidic supernatant and in the 40-80% ammonium sulfate fractions, was equally apportioned between the 0.04 and 0.08 M NaCI DEAE fractions. After further purification of both DEAE fractions, the preparations were subjected to one- and two-dimensional electrophoresis, and individual polypeptides were analyzed by amino acid sequencing. Three PAGs, which differed in amino acid sequence and apparent molecular masses (62, 59, and 55 kDa), were detected, each containing several isoforms with different pls: caprine (c) PAG62 (pl: 5.1, 4.8), cPAG59 (pl: 6.2, 5.9, 5.6), and cPAG55 (pl: 5.3, 5.1, 4.9). These proteins had high sequence identities to each other and to PAGs purified from other species. Each had two putative N-glycosylation sites within the 27 amino terminal residues sequenced. This work demonstrates that PAGs are present in goat placenta and that multiple forms are expressed. |
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Palavras-Chave: |
PAGs; Pregnancy-associated glycoproteins; Proteína placentária. |
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Thesagro: |
Caprino; Glicoproteína; Placenta; Prenhez; Reprodução. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02168naa a2200289 a 4500
001 1528835
005 2016-10-03
008 1998 bl uuuu u00u1 u #d
100 1 $aGARBAYO, J. M.
245 $aIsolation and partial characterization of a pregnancy-associated glycoprotein family from the goat placenta.
260 $c1998
520 $aAntigen(s) immunologically related to pregnancy-associated glycoproteins (PAGs) have previously been detected in the serum of pregnant goats. In this work, we describe a partial characterization of a family of PAGs isolated from the placenta of the goat. The procedure, monitored by RIA, included extraction of proteins at neutral pH, acidic, and ammonium sulfate precipitations; and gel filtration and ion exchange chromatographies. Immunoreactivity, initially located in the acidic supernatant and in the 40-80% ammonium sulfate fractions, was equally apportioned between the 0.04 and 0.08 M NaCI DEAE fractions. After further purification of both DEAE fractions, the preparations were subjected to one- and two-dimensional electrophoresis, and individual polypeptides were analyzed by amino acid sequencing. Three PAGs, which differed in amino acid sequence and apparent molecular masses (62, 59, and 55 kDa), were detected, each containing several isoforms with different pls: caprine (c) PAG62 (pl: 5.1, 4.8), cPAG59 (pl: 6.2, 5.9, 5.6), and cPAG55 (pl: 5.3, 5.1, 4.9). These proteins had high sequence identities to each other and to PAGs purified from other species. Each had two putative N-glycosylation sites within the 27 amino terminal residues sequenced. This work demonstrates that PAGs are present in goat placenta and that multiple forms are expressed.
650 $aCaprino
650 $aGlicoproteína
650 $aPlacenta
650 $aPrenhez
650 $aReprodução
653 $aPAGs
653 $aPregnancy-associated glycoproteins
653 $aProteína placentária
700 1 $aREMY, B.
700 1 $aALABART, J. L.
700 1 $aFOLCH, J.
700 1 $aWATTIEZ, R.
700 1 $aFALMAGNE, P.
700 1 $aBECKERS, J. F.
773 $tBiology of Reproduction$gv. 58, n. 1, p.109-115, 1998.
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Embrapa Caprinos e Ovinos (CNPC) |
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