The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase
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منابع مشابه
The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase.
The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase, comprising 363 residues, was determined. The sequence was deduced by automated sequencing of CNBr-cleavage, o-iodosobenzoic acid-cleavage, trypsin-digest and staphylococcal-proteinase-digest fragments. Comparison of the sequence with other class I aldolase sequences shows that the mammalian muscle isoenzym...
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The complete amino acid sequence of chicken skeletal-muscle enolase, comprising 433 residues, was determined. The sequence was deduced by automated sequencing of hydroxylamine-cleavage, CNBr-cleavage, o-iodosobenzoic acid-cleavage, clostripain-digest and staphylococcal-proteinase-digest fragments. The presence of several acid-labile peptide bonds and the tenacious aggregation of most CNBr-cleav...
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The complete amino-acid sequence of actin of rabbit skeletal muscle was determined. The actin polypeptide chain is composed of 374 residues, including one residue of the unusual amino acid N(r)-methyl histidine, and has a calculated molecular weight of 41,785. The sequence of actin was determined by isolating the peptides produced by cleavage of the protein with cyanogen bromide, determining th...
متن کاملALDOB (aldolase B, fructose-bisphosphate)
Other names: ALDB, EC 4.1.2.13, OTTHUMP00000021803 HGNC (Hugo): ALDOB Location: 9q31.1 Local order: Telomeric to the PRG-3 (plasticity related gene 3), BAAT (bile acid Coenzyme A: amino acid N-acyltransferase), MRPL50 (mitochondrial ribosomal protein L50) and ZNF189 (zinc finger protein 189) genes. Centromeric to C9orf125 (chromosome 9 open reading frame 125), RNF20 (ring finger protein 20), PP...
متن کاملPurification and amino acid sequence of fructose-1,6-bisphosphate aldolase from the electric organ of Electrophorus electricus (L.).
A soluble fructose-1,6-bisphosphate aldolase enzyme has been purified 50.2-fold (2.36%) at the homogeneity from the electric organ of Electrophorus electricus by one step of DEAE-52 anion exchange chromatography followed by Superose-12 gel filtration-FPLC. Like other aldolase enzymes the E. electricus protein is a dimer with two identical subunits of 45 kDa. The N-terminal (20 residues) reveale...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1988
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2490779