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...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1993-09, Vol.268 (25), p.18435-18437
Main Authors: Kenyon, K., Modi, W.S., Contente, S., Friedman, R.M.
Format: Article
Language:English
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
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)46643-9