A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25

A novel human cDNA with a predicted protein homologous to the carboxyl end of lysyl oxidase, an extracellular enzyme involved in the maturation of collagen and elastin, has been isolated. The homology to lysyl oxidase begins exactly at the position of the exon 1/exon 2 boundary in the mouse gene (Co...

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Published inThe Journal of biological chemistry Vol. 268; no. 25; pp. 18435 - 18437
Main Authors Kenyon, K., Modi, W.S., Contente, S., Friedman, R.M.
Format Journal Article
LanguageEnglish
Published Bethesda, MD Elsevier Inc 05.09.1993
American Society for Biochemistry and Molecular Biology
Subjects
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Blotting, Southern
Chromosome Mapping
Chromosomes, Human, Pair 15
DNA - isolation & purification
DNA Probes
Enzymes and enzyme inhibitors
Exons
Fundamental and applied biological sciences. Psychology
Humans
Mice
Molecular Sequence Data
Nucleic Acid Hybridization
Oxidoreductases
Poly A - genetics
Protein Biosynthesis
Protein-Lysine 6-Oxidase - chemistry
Protein-Lysine 6-Oxidase - genetics
RNA - genetics
RNA, Messenger
Sequence Homology, Nucleic Acid
Human
Complementary DNA
C terminal peptide
In situ
Oxidoreductases
Comparative study
Aminoacid sequence
Online AccessGet full text
ISSN0021-9258
1083-351X
DOI10.1016/S0021-9258(17)46643-9

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Abstract A novel human cDNA with a predicted protein homologous to the carboxyl end of lysyl oxidase, an extracellular enzyme involved in the maturation of collagen and elastin, has been isolated. The homology to lysyl oxidase begins exactly at the position of the exon 1/exon 2 boundary in the mouse gene (Contente, S., Csiszar, K., Kenyon, K., and Friedman, R. M. (1993) Genomics 16, 395-400). This lysyl oxidase-like gene, which appears to be no larger than 22.1 kilobases, codes for a single polyadenylated RNA species of 2.48 kilobases and has been mapped to chromosome 15q24-q25.
AbstractList A novel human cDNA with a predicted protein homologous to the carboxyl end of lysyl oxidase, an extracellular enzyme involved in the maturation of collagen and elastin, has been isolated. The homology to lysyl oxidase begins exactly at the position of the exon 1/exon 2 boundary in the mouse gene (Contente, S., Csiszar, K., Kenyon, K., and Friedman, R. M. (1993) Genomics 16, 395-400). This lysyl oxidase-like gene, which appears to be no larger than 22.1 kilobases, codes for a single polyadenylated RNA species of 2.48 kilobases and has been mapped to chromosome 15q24-q25.
A novel human cDNA with a predicted protein homologous to the carboxyl end of lysyl oxidase, an extracellular enzyme involved in the maturation of collagen and elastin, has been isolated. The homology to lysyl oxidase begins exactly at the position of the exon 1/exon 2 boundary in the mouse gene (Contente, S., Csiszar, K., Kenyon, K., and Friedman, R. M. (1993) Genomics 16, 395-400). This lysyl oxidase-like gene, which appears to be no larger than 22.1 kilobases, codes for a single polyadenylated RNA species of 2.48 kilobases and has been mapped to chromosome 15q24-q25.A novel human cDNA with a predicted protein homologous to the carboxyl end of lysyl oxidase, an extracellular enzyme involved in the maturation of collagen and elastin, has been isolated. The homology to lysyl oxidase begins exactly at the position of the exon 1/exon 2 boundary in the mouse gene (Contente, S., Csiszar, K., Kenyon, K., and Friedman, R. M. (1993) Genomics 16, 395-400). This lysyl oxidase-like gene, which appears to be no larger than 22.1 kilobases, codes for a single polyadenylated RNA species of 2.48 kilobases and has been mapped to chromosome 15q24-q25.
A novel human cDNA with a predicted protein homologous to the carboxyl end of lysyl oxidase, an extracellular enzyme involved in the maturation of collagen and elastin, has been isolated. The homology to lysyl oxidase begins exactly at the position of the exon 1/exon 2 boundary in the mouse gene. This lysyl oxidase-like gene, which appears to be no larger than 22.1 kilobases, codes for a single polyadenylated RNA species of 2.48 kilobases and has been mapped to chromosome 15q24-q25.
A novel human cDNA with a predicted protein homologous to the carboxyl end of lysyl oxidase, an extracellular enzyme involved in the maturation of collagen and elastin, has been isolated. The homology to lysyl oxidase begins exactly at the position of the exon 1/exon 2 boundary in the mouse gene (Contente, S., Csiszar, K., Kenyon, K., and Friedman, R. M. (1993) Genomics 16, 395-400). This lysyl oxidase-like gene, which appears to be no larger than 22.1 kilobases, codes for a single polyadenylated RNA species of 2.48 kilobases and has been mapped to chromosome 15q24-q25.
Author Kenyon, K.
Contente, S.
Friedman, R.M.
Modi, W.S.
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  surname: Friedman
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Issue 25
Keywords Human
Complementary DNA
C terminal peptide
In situ
Oxidoreductases
Comparative study
Aminoacid sequence
Language English
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Snippet A novel human cDNA with a predicted protein homologous to the carboxyl end of lysyl oxidase, an extracellular enzyme involved in the maturation of collagen and...
A novel human cDNA with a predicted protein homologous to the carboxyl end of lysyl oxidase, an extracellular enzyme involved in the maturation of collagen and...
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SubjectTerms Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Blotting, Southern
Chromosome Mapping
Chromosomes, Human, Pair 15
DNA - isolation & purification
DNA Probes
Enzymes and enzyme inhibitors
Exons
Fundamental and applied biological sciences. Psychology
Humans
Mice
Molecular Sequence Data
Nucleic Acid Hybridization
Oxidoreductases
Poly A - genetics
Protein Biosynthesis
Protein-Lysine 6-Oxidase - chemistry
Protein-Lysine 6-Oxidase - genetics
RNA - genetics
RNA, Messenger
Sequence Homology, Nucleic Acid
Title A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25
URI https://dx.doi.org/10.1016/S0021-9258(17)46643-9
http://www.jbc.org/content/268/25/18435.abstract
https://www.ncbi.nlm.nih.gov/pubmed/7689553
https://www.proquest.com/docview/16774502
https://www.proquest.com/docview/75924067
Volume 268
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