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Title: Molecular cloning and nucleotide sequence of cDNA for human liver arginase

Abstract

Arginase (EC3.5.3.1) catalyzes the last step of the urea cycle in the liver of ureotelic animals. Inherited deficiency of the enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia. To facilitate investigation of the enzyme and gene structures and to elucidate the nature of the mutation in argininemia, the authors isolated cDNA clones for human liver arginase. Oligo(dT)-primed and random primer human liver cDNA libraries in lambda gt11 were screened using isolated rat arginase cDNA as a probe. Two of the positive clones, designated lambda hARG6 and lambda hARG109, contained an overlapping cDNA sequence with an open reading frame encoding a polypeptide of 322 amino acid residues (predicted M/sub r/, 34,732), a 5'-untranslated sequence of 56 base pairs, a 3'-untranslated sequence of 423 base pairs, and a poly(A) segment. Arginase activity was detected in Escherichia coli cells transformed with the plasmid carrying lambda hARG6 cDNA insert. RNA gel blot analysis of human liver RNA showed a single mRNA of 1.6 kilobases. The predicted amino acid sequence of human liver arginase is 87% and 41% identical with those of the rat liver and yeast enzymes, respectively. There are several highly conserved segments among the human, rat, and yeast enzymes.

Authors:
; ; ; ; ;
Publication Date:
Research Org.:
Kumamoto Univ. Medical School, Japan
OSTI Identifier:
6022635
Resource Type:
Journal Article
Journal Name:
Proc. Natl. Acad. Sci. U.S.A.; (United States)
Additional Journal Information:
Journal Volume: 84:2
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ARGINASE; AMINO ACID SEQUENCE; GENETIC MAPPING; RECOMBINANT DNA; DNA SEQUENCING; BIOLOGICAL PATHWAYS; ESCHERICHIA COLI; HEREDITARY DISEASES; LIVER; MAN; MESSENGER-RNA; PHOSPHORUS 32; RATS; UREA; AMIDASES; AMIDES; ANIMALS; BACTERIA; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; BODY; CARBONIC ACID DERIVATIVES; DAYS LIVING RADIOISOTOPES; DIGESTIVE SYSTEM; DISEASES; DNA; ENZYMES; GLANDS; HYDROLASES; ISOTOPES; LIGHT NUCLEI; MAMMALS; MAPPING; MICROORGANISMS; MOLECULAR STRUCTURE; NON-PEPTIDE C-N HYDROLASES; NUCLEI; NUCLEIC ACIDS; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; ORGANS; PHOSPHORUS ISOTOPES; PRIMATES; RADIOISOTOPES; RNA; RODENTS; STRUCTURAL CHEMICAL ANALYSIS; VERTEBRATES; 550401* - Genetics- Tracer Techniques; 550201 - Biochemistry- Tracer Techniques

Citation Formats

Haraguchi, Y, Takiguchi, M, Amaya, Y, Kawamoto, S, Matsuda, I, and Mori, M. Molecular cloning and nucleotide sequence of cDNA for human liver arginase. United States: N. p., 1987. Web. doi:10.1073/pnas.84.2.412.
Haraguchi, Y, Takiguchi, M, Amaya, Y, Kawamoto, S, Matsuda, I, & Mori, M. Molecular cloning and nucleotide sequence of cDNA for human liver arginase. United States. https://doi.org/10.1073/pnas.84.2.412
Haraguchi, Y, Takiguchi, M, Amaya, Y, Kawamoto, S, Matsuda, I, and Mori, M. 1987. "Molecular cloning and nucleotide sequence of cDNA for human liver arginase". United States. https://doi.org/10.1073/pnas.84.2.412.
@article{osti_6022635,
title = {Molecular cloning and nucleotide sequence of cDNA for human liver arginase},
author = {Haraguchi, Y and Takiguchi, M and Amaya, Y and Kawamoto, S and Matsuda, I and Mori, M},
abstractNote = {Arginase (EC3.5.3.1) catalyzes the last step of the urea cycle in the liver of ureotelic animals. Inherited deficiency of the enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia. To facilitate investigation of the enzyme and gene structures and to elucidate the nature of the mutation in argininemia, the authors isolated cDNA clones for human liver arginase. Oligo(dT)-primed and random primer human liver cDNA libraries in lambda gt11 were screened using isolated rat arginase cDNA as a probe. Two of the positive clones, designated lambda hARG6 and lambda hARG109, contained an overlapping cDNA sequence with an open reading frame encoding a polypeptide of 322 amino acid residues (predicted M/sub r/, 34,732), a 5'-untranslated sequence of 56 base pairs, a 3'-untranslated sequence of 423 base pairs, and a poly(A) segment. Arginase activity was detected in Escherichia coli cells transformed with the plasmid carrying lambda hARG6 cDNA insert. RNA gel blot analysis of human liver RNA showed a single mRNA of 1.6 kilobases. The predicted amino acid sequence of human liver arginase is 87% and 41% identical with those of the rat liver and yeast enzymes, respectively. There are several highly conserved segments among the human, rat, and yeast enzymes.},
doi = {10.1073/pnas.84.2.412},
url = {https://www.osti.gov/biblio/6022635}, journal = {Proc. Natl. Acad. Sci. U.S.A.; (United States)},
number = ,
volume = 84:2,
place = {United States},
year = {Thu Jan 01 00:00:00 EST 1987},
month = {Thu Jan 01 00:00:00 EST 1987}
}