Nucleotide sequence of rat liver aldolase B messenger RNA. 1984

K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa

The nucleotide sequence of messenger RNA encoding rat liver aldolase B has been determined by sequence analysis using recombinant cDNAs cloned in bacterial plasmids. The sequence contains part of the 5'-untranslatable region (68 nucleotides), the entire coding region (1092 nucleotides), and the complete 3'-untranslatable region (387 nucleotides), excluding the poly(A) tail. A potential ribosomal-binding site is located about 30 nucleotides upstream from the initiation codon. The amino acid sequence of rat liver aldolase B is composed of 364 amino acids and has 70% homology with rabbit muscle aldolase A.

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D003062 Codon A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE). Codon, Sense,Sense Codon,Codons,Codons, Sense,Sense Codons
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D004262 DNA Restriction Enzymes Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1. Restriction Endonucleases,DNA Restriction Enzyme,Restriction Endonuclease,Endonuclease, Restriction,Endonucleases, Restriction,Enzymes, DNA Restriction,Restriction Enzyme, DNA,Restriction Enzymes, DNA
D005634 Fructose-Bisphosphate Aldolase An enzyme of the lyase class that catalyzes the cleavage of fructose 1,6-biphosphate to form dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The enzyme also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. (Enzyme Nomenclature, 1992) E.C. 4.1.2.13. Aldolase,Fructosediphosphate Aldolase,Aldolase A,Aldolase B,Aldolase C,Fructose 1,6-Bisphosphate Aldolase,Fructose 1,6-Bisphosphate Aldolase, Class II,Fructose 1-Phosphate Aldolase,Fructose Biphosphate Aldolase,Fructosemonophosphate Aldolase,1,6-Bisphosphate Aldolase, Fructose,Aldolase, Fructose 1,6-Bisphosphate,Aldolase, Fructose 1-Phosphate,Aldolase, Fructose Biphosphate,Aldolase, Fructose-Bisphosphate,Aldolase, Fructosediphosphate,Aldolase, Fructosemonophosphate,Fructose 1 Phosphate Aldolase,Fructose 1,6 Bisphosphate Aldolase,Fructose Bisphosphate Aldolase
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA

Related Publications

K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa
May 1981, Biochemical and biophysical research communications,
K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa
August 1985, Biochemical and biophysical research communications,
K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa
January 1984, The Journal of biological chemistry,
K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa
January 1981, Proceedings of the National Academy of Sciences of the United States of America,
K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa
January 1985, Gene,
K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa
November 1981, The Journal of biological chemistry,
K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa
October 1984, Biochemical and biophysical research communications,
K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa
January 1982, Biochemical and biophysical research communications,
K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa
January 1982, Molecular and cellular endocrinology,
K Tsutsumi, and T Mukai, and R Tsutsumi, and M Mori, and M Daimon, and T Tanaka, and H Yatsuki, and K Hori, and K Ishikawa
January 1977, Hemoglobin,
Copied contents to your clipboard!