Structural Characterization of Cytosolic IMADP+-Dependent Isocitrate Dehydrogenase from Rat Ovary
| Autor: | Jennings Gt, Parmelee D, Roller Pp, Sechi S |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Isocitrates
Protein Denaturation Protein Folding IDH1 Protein Conformation Molecular Sequence Data Ovary Biochemistry Protein Structure Secondary Cytosol medicine Animals Amino Acid Sequence Chromatography High Pressure Liquid Sequence Homology Amino Acid Chemistry Circular Dichroism Temperature Isocitrate Dehydrogenase Rats medicine.anatomical_structure Isocitrate dehydrogenase Female Sequence Analysis |
| Zdroj: | Enzyme and Protein. 48:27-36 |
| ISSN: | 2504-2556 1019-6773 |
| DOI: | 10.1159/000474966 |
| Popis: | Cytosolic NADP(+)-dependent isocitrate dehydrogenase was purified to homogeneity from superovulated rat ovaries. Amino acid sequence information was obtained by analyzing peptides generated by digestion with either cyanogen bromide or trypsin. Eleven peptides were sequenced and a total of 146 amino acids were identified. Nine of these peptides were found to be 60-100% identical with sequences from mitochondrial NADP(+)-dependent isocitrate dehydrogenase. Conservation of amino acids was observed for residues that were previously identified as potentially binding isocitrate-Mg2+. Circular dichroism measurements showed that the structure is composed of approximately 35% alpha-helix and 21% beta-sheet segments. Temperature denaturation studies indicated that the enzyme is more stable in the presence of isocitrate. |
| Databáze: | OpenAIRE |
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