xP1 and xP4. P-domain peptides expressed in Xenopus laevis stomach mucosa

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Standard

xP1 and xP4. P-domain peptides expressed in Xenopus laevis stomach mucosa. / Hauser, F; Hoffmann, W.

In: The Journal of Biological Chemistry, Vol. 266, No. 31, 05.11.1991, p. 21306-9.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hauser, F & Hoffmann, W 1991, 'xP1 and xP4. P-domain peptides expressed in Xenopus laevis stomach mucosa', The Journal of Biological Chemistry, vol. 266, no. 31, pp. 21306-9.

APA

Hauser, F., & Hoffmann, W. (1991). xP1 and xP4. P-domain peptides expressed in Xenopus laevis stomach mucosa. The Journal of Biological Chemistry, 266(31), 21306-9.

Vancouver

Hauser F, Hoffmann W. xP1 and xP4. P-domain peptides expressed in Xenopus laevis stomach mucosa. The Journal of Biological Chemistry. 1991 Nov 5;266(31):21306-9.

Author

Hauser, F ; Hoffmann, W. / xP1 and xP4. P-domain peptides expressed in Xenopus laevis stomach mucosa. In: The Journal of Biological Chemistry. 1991 ; Vol. 266, No. 31. pp. 21306-9.

Bibtex

@article{f116c29e9867499cb8d9c65942ae836b,
title = "xP1 and xP4. P-domain peptides expressed in Xenopus laevis stomach mucosa",
abstract = "Two different precursors for secretory polypeptides from the stomach of Xenopus laevis have been characterized by cDNA cloning. Both mature polypeptides are potential candidates for gastrointestinal growth factors. One, xP1, is the X. laevis homologue of the pS2 gene product consisting only of a single P-domain, whereas the second, xP4, is a novel polypeptide formed by four P-domains arranged in tandem. Northern analysis detected both transcripts in the stomach but not in the skin or the brain. In situ hybridizations localized the expression of both precursors in surface mucous cells of the gastric mucosa. With an antibody generated against the deduced C-terminal end of xP4, the mature polypeptide was investigated by Western analysis revealing N-glycosylation of xP4.",
keywords = "Amino Acid Sequence, Animals, Base Sequence, Blotting, Northern, Cloning, Molecular, DNA/genetics, Gastric Mucosa/physiology, Gene Expression, Growth Substances/genetics, Intercellular Signaling Peptides and Proteins, Molecular Sequence Data, Mucins/genetics, Nucleic Acid Hybridization, Oligonucleotides/chemistry, RNA, Messenger/genetics, Sequence Alignment, Xenopus Proteins, Xenopus laevis/genetics",
author = "F Hauser and W Hoffmann",
year = "1991",
month = nov,
day = "5",
language = "English",
volume = "266",
pages = "21306--9",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "31",

}

RIS

TY - JOUR

T1 - xP1 and xP4. P-domain peptides expressed in Xenopus laevis stomach mucosa

AU - Hauser, F

AU - Hoffmann, W

PY - 1991/11/5

Y1 - 1991/11/5

N2 - Two different precursors for secretory polypeptides from the stomach of Xenopus laevis have been characterized by cDNA cloning. Both mature polypeptides are potential candidates for gastrointestinal growth factors. One, xP1, is the X. laevis homologue of the pS2 gene product consisting only of a single P-domain, whereas the second, xP4, is a novel polypeptide formed by four P-domains arranged in tandem. Northern analysis detected both transcripts in the stomach but not in the skin or the brain. In situ hybridizations localized the expression of both precursors in surface mucous cells of the gastric mucosa. With an antibody generated against the deduced C-terminal end of xP4, the mature polypeptide was investigated by Western analysis revealing N-glycosylation of xP4.

AB - Two different precursors for secretory polypeptides from the stomach of Xenopus laevis have been characterized by cDNA cloning. Both mature polypeptides are potential candidates for gastrointestinal growth factors. One, xP1, is the X. laevis homologue of the pS2 gene product consisting only of a single P-domain, whereas the second, xP4, is a novel polypeptide formed by four P-domains arranged in tandem. Northern analysis detected both transcripts in the stomach but not in the skin or the brain. In situ hybridizations localized the expression of both precursors in surface mucous cells of the gastric mucosa. With an antibody generated against the deduced C-terminal end of xP4, the mature polypeptide was investigated by Western analysis revealing N-glycosylation of xP4.

KW - Amino Acid Sequence

KW - Animals

KW - Base Sequence

KW - Blotting, Northern

KW - Cloning, Molecular

KW - DNA/genetics

KW - Gastric Mucosa/physiology

KW - Gene Expression

KW - Growth Substances/genetics

KW - Intercellular Signaling Peptides and Proteins

KW - Molecular Sequence Data

KW - Mucins/genetics

KW - Nucleic Acid Hybridization

KW - Oligonucleotides/chemistry

KW - RNA, Messenger/genetics

KW - Sequence Alignment

KW - Xenopus Proteins

KW - Xenopus laevis/genetics

M3 - Journal article

C2 - 1939167

VL - 266

SP - 21306

EP - 21309

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 31

ER -

ID: 347886162