Subunit structure of rabbit muscle aldolase: Extent of homology of the α and β subunits and age-dependent changes in their ratio
Autor: | M. Koida, B.L. Horecker, C.Y. Lai |
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Rok vydání: | 1969 |
Předmět: |
Male
Aging Protein subunit Biophysics Peptide Carboxypeptidases Biochemistry Chromatography DEAE-Cellulose Homology (biology) chemistry.chemical_compound Fructose-Bisphosphate Aldolase medicine Animals Urea Histidine Trypsin Amino Acids Molecular Biology chemistry.chemical_classification Cyanides biology Muscles Aldolase A Skeletal muscle Bromine Electrophoresis Disc Molecular biology Amino acid medicine.anatomical_structure chemistry Chromatography Gel biology.protein Tyrosine Female Cyanogen bromide Rabbits Peptides |
Zdroj: | Archives of Biochemistry and Biophysics. 134:623-631 |
ISSN: | 0003-9861 |
DOI: | 10.1016/0003-9861(69)90326-9 |
Popis: | The α and β subunits of rabbit muscle aldolase, dissociated in 8 m urea and separated by chromatography on DEAE-cellulose, were cleaved with cyanogen bromide. The corresponding cyanogen bromide peptides from the two subunits were found to be very similar in amino acid composition and in tryptic fingerprints, possibly differing in only a single peptide. In aldolase prepared from skeletal muscle of young rabbits the α subunit predominates, in contrast to preparations from adult rabbits which contain nearly equal quantities of the α and β subunits. The change in ratio occurs between 3 and 5 months of age. These results suggest that the two subunits have a common genetic origin, and that the β subunit may arise by a modification of one or more amino acids near the COOH-terminus of the molecule. |
Databáze: | OpenAIRE |
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