Prolyl iminopeptidase from seeds of sunflower (Helianthus annuus L.) |
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| Authors: | Kiril Tishinov Svetla Petrova Peter Nedkov |
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| Institution: | 1. Laboratory of Chemistry and Biophysics of Proteins and Enzymes, Institute of Organic Chemistry with Centre of Phytochemistry, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., Block 9, 1113, Sofia, Bulgaria
2. Department of Biochemistry, Faculty of Biology, Sofia University, 8 Dragan Tsankov Blvd., 1164, Sofia, Bulgaria
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| Abstract: | Prolyl iminopeptidase from sunflower seed (Helianthus annuus L.) was purified to molecular homogeneity. It is a 105-kDa heterodimer consisting of two subunits: 53 and 55 kDa. It has pI of 6.2 and optimal activity at pH 8.0–8.5 and 45–50°C. The inhibitory analysis was inconclusive about its catalytic machinery, as a significant degree of modification was not observed with any of the used diagnostic inhibitors. Its specificity is restricted to removal of N-terminal prolyl residues. |
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