P-domains as shuffled cysteine-rich modules in integumentary mucin C.1 (FIM-C.1) from Xenopus laevis. Polydispersity and genetic polymorphism

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Standard

P-domains as shuffled cysteine-rich modules in integumentary mucin C.1 (FIM-C.1) from Xenopus laevis. Polydispersity and genetic polymorphism. / Hauser, F; Hoffmann, W.

In: The Journal of Biological Chemistry, Vol. 267, No. 34, 05.12.1992, p. 24620-4.

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

Harvard

Hauser, F & Hoffmann, W 1992, 'P-domains as shuffled cysteine-rich modules in integumentary mucin C.1 (FIM-C.1) from Xenopus laevis. Polydispersity and genetic polymorphism', The Journal of Biological Chemistry, vol. 267, no. 34, pp. 24620-4.

APA

Hauser, F., & Hoffmann, W. (1992). P-domains as shuffled cysteine-rich modules in integumentary mucin C.1 (FIM-C.1) from Xenopus laevis. Polydispersity and genetic polymorphism. The Journal of Biological Chemistry, 267(34), 24620-4.

Vancouver

Hauser F, Hoffmann W. P-domains as shuffled cysteine-rich modules in integumentary mucin C.1 (FIM-C.1) from Xenopus laevis. Polydispersity and genetic polymorphism. The Journal of Biological Chemistry. 1992 Dec 5;267(34):24620-4.

Author

Hauser, F ; Hoffmann, W. / P-domains as shuffled cysteine-rich modules in integumentary mucin C.1 (FIM-C.1) from Xenopus laevis. Polydispersity and genetic polymorphism. In: The Journal of Biological Chemistry. 1992 ; Vol. 267, No. 34. pp. 24620-4.

Bibtex

@article{30ab5a3939214a0883c2d5799c9543a6,
title = "P-domains as shuffled cysteine-rich modules in integumentary mucin C.1 (FIM-C.1) from Xenopus laevis. Polydispersity and genetic polymorphism",
abstract = "A new frog integumentary mucin (FIM-C.1) has been discovered by molecular cloning. This mucin contains at least six typical P-domains as cysteine-rich modules. Shuffled P-domains have previously been detected in FIM-A.1, and they also form the basis of various P-domain peptides, which presumably have growth-modulating activities. Furthermore, FIM-C.1 contains at least three threonine-rich clusters, which consist of semi-repetitive cassettes. Various polydisperse transcripts have been characterized. They originate from two genes only and differ by deletions/insertions that are congruent with the semi-repetitive cassettes. Thus, polydispersities are probably generated by alternative splicing. Southern analysis revealed genetic polymorphism between different individuals. Furthermore, a specific antiserum was generated against a synthetic peptide deduced from the COOH-terminal end of FIM-C.1 and used for Western analysis.",
keywords = "Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Codon/genetics, Cysteine, Molecular Sequence Data, Mucins/genetics, Oligodeoxyribonucleotides, Polymerase Chain Reaction, Polymorphism, Genetic, Restriction Mapping, Sequence Deletion, Sequence Homology, Amino Acid, Templates, Genetic, Xenopus Proteins, Xenopus laevis",
author = "F Hauser and W Hoffmann",
year = "1992",
month = dec,
day = "5",
language = "English",
volume = "267",
pages = "24620--4",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "34",

}

RIS

TY - JOUR

T1 - P-domains as shuffled cysteine-rich modules in integumentary mucin C.1 (FIM-C.1) from Xenopus laevis. Polydispersity and genetic polymorphism

AU - Hauser, F

AU - Hoffmann, W

PY - 1992/12/5

Y1 - 1992/12/5

N2 - A new frog integumentary mucin (FIM-C.1) has been discovered by molecular cloning. This mucin contains at least six typical P-domains as cysteine-rich modules. Shuffled P-domains have previously been detected in FIM-A.1, and they also form the basis of various P-domain peptides, which presumably have growth-modulating activities. Furthermore, FIM-C.1 contains at least three threonine-rich clusters, which consist of semi-repetitive cassettes. Various polydisperse transcripts have been characterized. They originate from two genes only and differ by deletions/insertions that are congruent with the semi-repetitive cassettes. Thus, polydispersities are probably generated by alternative splicing. Southern analysis revealed genetic polymorphism between different individuals. Furthermore, a specific antiserum was generated against a synthetic peptide deduced from the COOH-terminal end of FIM-C.1 and used for Western analysis.

AB - A new frog integumentary mucin (FIM-C.1) has been discovered by molecular cloning. This mucin contains at least six typical P-domains as cysteine-rich modules. Shuffled P-domains have previously been detected in FIM-A.1, and they also form the basis of various P-domain peptides, which presumably have growth-modulating activities. Furthermore, FIM-C.1 contains at least three threonine-rich clusters, which consist of semi-repetitive cassettes. Various polydisperse transcripts have been characterized. They originate from two genes only and differ by deletions/insertions that are congruent with the semi-repetitive cassettes. Thus, polydispersities are probably generated by alternative splicing. Southern analysis revealed genetic polymorphism between different individuals. Furthermore, a specific antiserum was generated against a synthetic peptide deduced from the COOH-terminal end of FIM-C.1 and used for Western analysis.

KW - Amino Acid Sequence

KW - Animals

KW - Base Sequence

KW - Cloning, Molecular

KW - Codon/genetics

KW - Cysteine

KW - Molecular Sequence Data

KW - Mucins/genetics

KW - Oligodeoxyribonucleotides

KW - Polymerase Chain Reaction

KW - Polymorphism, Genetic

KW - Restriction Mapping

KW - Sequence Deletion

KW - Sequence Homology, Amino Acid

KW - Templates, Genetic

KW - Xenopus Proteins

KW - Xenopus laevis

M3 - Journal article

C2 - 1447205

VL - 267

SP - 24620

EP - 24624

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 34

ER -

ID: 347885984