Purification and properties of two isozymes of pyruvate kinase from Mucor racemosus
| Autor: | T M Hohn, J L Paznokas |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Mucor
biology Molecular mass urogenital system Mucor racemosus Pyruvate Kinase biology.organism_classification Peptide Mapping Microbiology Isozyme Yeast Isoenzymes Molecular Weight chemistry.chemical_compound Biochemistry chemistry Electrophoresis Polyacrylamide Gel Cyanogen bromide Amino Acids Molecular Biology Polyacrylamide gel electrophoresis Pyruvate kinase Research Article |
| Zdroj: | Journal of Bacteriology. 169:3525-3530 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.169.8.3525-3530.1987 |
| Popis: | The dimorphic phycomycete Mucor racemosus was found to contain up to five electrophoretic forms of pyruvate kinase (ATP: pyruvate 2-O-phosphotransferase, EC 2.7.1.40) depending on growth conditions. M. racemosus hyphal cells grown on glutamic acid as the carbon source contained only the fastest electrophoretic form, designated PK1, while yeast cells grown on glucose contained only the slowest electrophoretic form, PK5. Intermediate electrophoretic forms PK2, PK3, and PK4 as well as PK1 and PK5 were found in hyphal cells grown on media containing fructose or cellibiose. All five electrophoretic forms had molecular weights of ca. 230,000 as determined from plots of log Rm versus acrylamide gel concentration. Both PK1 and PK5 were purified to homogeneity and determined to be homotetramers, with subunit molecular weights of 54,000 and 58,100, respectively. The amino acid content of PK1 and PK5 was determined and found to be similar but not identical. Analysis of limited tryptic digests and cyanogen bromide cleavage fragments of PK1 and PK5 indicate that the subunits of the two isozymes are significantly different. |
| Databáze: | OpenAIRE |
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