The complete sequence of a novel human pituitary glycopeptide homologous to pig posterior pituitary glycopeptide
The isolation and complete purification of a novel human pituitary glycopeptide (HPGP) from whole pituitaries is described. Amino acid composition predicts a glycopeptide rich in glucosamine. Complete sequence determination showed it to be a 39 residues with an oligosaccharide chain attached at Asn...
Ausführliche Beschreibung
Autor*in: |
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E-Artikel |
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Sprache: |
Englisch |
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1981 |
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Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 100(1981), 2, Seite 901-907 |
Übergeordnetes Werk: |
volume:100 ; year:1981 ; number:2 ; pages:901-907 |
Links: |
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NLEJ176953663 |
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520 | |a The isolation and complete purification of a novel human pituitary glycopeptide (HPGP) from whole pituitaries is described. Amino acid composition predicts a glycopeptide rich in glucosamine. Complete sequence determination showed it to be a 39 residues with an oligosaccharide chain attached at Asn residue No. 6. It exhibits marked sequence homology to previously isolated pig posterior pituitary glycopeptide and to whole pituitary glycopeptides isolated from ox, sheep and pig. Based on these results and the presence of such a peptide in posterior pituitary it is suggested that it could form part of the N-terminal glycopeptide extension of the precursor of neurophysin-arginine vasopressin. | ||
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(DE-627)NLEJ176953663 (DE-599)GBVNLZ176953663 DE-627 ger DE-627 rakwb eng The complete sequence of a novel human pituitary glycopeptide homologous to pig posterior pituitary glycopeptide 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The isolation and complete purification of a novel human pituitary glycopeptide (HPGP) from whole pituitaries is described. Amino acid composition predicts a glycopeptide rich in glucosamine. Complete sequence determination showed it to be a 39 residues with an oligosaccharide chain attached at Asn residue No. 6. It exhibits marked sequence homology to previously isolated pig posterior pituitary glycopeptide and to whole pituitary glycopeptides isolated from ox, sheep and pig. Based on these results and the presence of such a peptide in posterior pituitary it is suggested that it could form part of the N-terminal glycopeptide extension of the precursor of neurophysin-arginine vasopressin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Seidah, N.G. oth Benjannet, S. oth Chretien, M. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 100(1981), 2, Seite 901-907 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:100 year:1981 number:2 pages:901-907 http://dx.doi.org/10.1016/S0006-291X(81)80258-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 100 1981 2 901-907 |
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(DE-627)NLEJ176953663 (DE-599)GBVNLZ176953663 DE-627 ger DE-627 rakwb eng The complete sequence of a novel human pituitary glycopeptide homologous to pig posterior pituitary glycopeptide 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The isolation and complete purification of a novel human pituitary glycopeptide (HPGP) from whole pituitaries is described. Amino acid composition predicts a glycopeptide rich in glucosamine. Complete sequence determination showed it to be a 39 residues with an oligosaccharide chain attached at Asn residue No. 6. It exhibits marked sequence homology to previously isolated pig posterior pituitary glycopeptide and to whole pituitary glycopeptides isolated from ox, sheep and pig. Based on these results and the presence of such a peptide in posterior pituitary it is suggested that it could form part of the N-terminal glycopeptide extension of the precursor of neurophysin-arginine vasopressin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Seidah, N.G. oth Benjannet, S. oth Chretien, M. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 100(1981), 2, Seite 901-907 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:100 year:1981 number:2 pages:901-907 http://dx.doi.org/10.1016/S0006-291X(81)80258-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 100 1981 2 901-907 |
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(DE-627)NLEJ176953663 (DE-599)GBVNLZ176953663 DE-627 ger DE-627 rakwb eng The complete sequence of a novel human pituitary glycopeptide homologous to pig posterior pituitary glycopeptide 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The isolation and complete purification of a novel human pituitary glycopeptide (HPGP) from whole pituitaries is described. Amino acid composition predicts a glycopeptide rich in glucosamine. Complete sequence determination showed it to be a 39 residues with an oligosaccharide chain attached at Asn residue No. 6. It exhibits marked sequence homology to previously isolated pig posterior pituitary glycopeptide and to whole pituitary glycopeptides isolated from ox, sheep and pig. Based on these results and the presence of such a peptide in posterior pituitary it is suggested that it could form part of the N-terminal glycopeptide extension of the precursor of neurophysin-arginine vasopressin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Seidah, N.G. oth Benjannet, S. oth Chretien, M. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 100(1981), 2, Seite 901-907 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:100 year:1981 number:2 pages:901-907 http://dx.doi.org/10.1016/S0006-291X(81)80258-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 100 1981 2 901-907 |
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(DE-627)NLEJ176953663 (DE-599)GBVNLZ176953663 DE-627 ger DE-627 rakwb eng The complete sequence of a novel human pituitary glycopeptide homologous to pig posterior pituitary glycopeptide 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The isolation and complete purification of a novel human pituitary glycopeptide (HPGP) from whole pituitaries is described. Amino acid composition predicts a glycopeptide rich in glucosamine. Complete sequence determination showed it to be a 39 residues with an oligosaccharide chain attached at Asn residue No. 6. It exhibits marked sequence homology to previously isolated pig posterior pituitary glycopeptide and to whole pituitary glycopeptides isolated from ox, sheep and pig. Based on these results and the presence of such a peptide in posterior pituitary it is suggested that it could form part of the N-terminal glycopeptide extension of the precursor of neurophysin-arginine vasopressin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Seidah, N.G. oth Benjannet, S. oth Chretien, M. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 100(1981), 2, Seite 901-907 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:100 year:1981 number:2 pages:901-907 http://dx.doi.org/10.1016/S0006-291X(81)80258-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 100 1981 2 901-907 |
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(DE-627)NLEJ176953663 (DE-599)GBVNLZ176953663 DE-627 ger DE-627 rakwb eng The complete sequence of a novel human pituitary glycopeptide homologous to pig posterior pituitary glycopeptide 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The isolation and complete purification of a novel human pituitary glycopeptide (HPGP) from whole pituitaries is described. Amino acid composition predicts a glycopeptide rich in glucosamine. Complete sequence determination showed it to be a 39 residues with an oligosaccharide chain attached at Asn residue No. 6. It exhibits marked sequence homology to previously isolated pig posterior pituitary glycopeptide and to whole pituitary glycopeptides isolated from ox, sheep and pig. Based on these results and the presence of such a peptide in posterior pituitary it is suggested that it could form part of the N-terminal glycopeptide extension of the precursor of neurophysin-arginine vasopressin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Seidah, N.G. oth Benjannet, S. oth Chretien, M. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 100(1981), 2, Seite 901-907 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:100 year:1981 number:2 pages:901-907 http://dx.doi.org/10.1016/S0006-291X(81)80258-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 100 1981 2 901-907 |
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complete sequence of a novel human pituitary glycopeptide homologous to pig posterior pituitary glycopeptide |
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The complete sequence of a novel human pituitary glycopeptide homologous to pig posterior pituitary glycopeptide |
abstract |
The isolation and complete purification of a novel human pituitary glycopeptide (HPGP) from whole pituitaries is described. Amino acid composition predicts a glycopeptide rich in glucosamine. Complete sequence determination showed it to be a 39 residues with an oligosaccharide chain attached at Asn residue No. 6. It exhibits marked sequence homology to previously isolated pig posterior pituitary glycopeptide and to whole pituitary glycopeptides isolated from ox, sheep and pig. Based on these results and the presence of such a peptide in posterior pituitary it is suggested that it could form part of the N-terminal glycopeptide extension of the precursor of neurophysin-arginine vasopressin. |
abstractGer |
The isolation and complete purification of a novel human pituitary glycopeptide (HPGP) from whole pituitaries is described. Amino acid composition predicts a glycopeptide rich in glucosamine. Complete sequence determination showed it to be a 39 residues with an oligosaccharide chain attached at Asn residue No. 6. It exhibits marked sequence homology to previously isolated pig posterior pituitary glycopeptide and to whole pituitary glycopeptides isolated from ox, sheep and pig. Based on these results and the presence of such a peptide in posterior pituitary it is suggested that it could form part of the N-terminal glycopeptide extension of the precursor of neurophysin-arginine vasopressin. |
abstract_unstemmed |
The isolation and complete purification of a novel human pituitary glycopeptide (HPGP) from whole pituitaries is described. Amino acid composition predicts a glycopeptide rich in glucosamine. Complete sequence determination showed it to be a 39 residues with an oligosaccharide chain attached at Asn residue No. 6. It exhibits marked sequence homology to previously isolated pig posterior pituitary glycopeptide and to whole pituitary glycopeptides isolated from ox, sheep and pig. Based on these results and the presence of such a peptide in posterior pituitary it is suggested that it could form part of the N-terminal glycopeptide extension of the precursor of neurophysin-arginine vasopressin. |
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