Selective and asymmetric action of trypsin on the dimeric forms of seminal Rnase
| Autor: | F. Dal Piaz, Piero Pucci, C. De Lorenzo, Giuseppe D'Alessio, A. Di Maro, Renata Piccoli |
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| Přispěvatelé: | DE LORENZO, Claudia, DAL PIAZ, F., Piccoli, R., DI MARO, A., Pucci, Pietro, D'Alessio, G., DE LORENZO, C., DI MARO, Antimo, Pucci, P., Piccoli, Renata |
| Rok vydání: | 1998 |
| Předmět: |
Male
Models Molecular Electrospray RNase P Stereochemistry Protein Conformation Sequence (biology) Biochemistry Hydrolysis Protein structure Ribonucleases BS-RNase Semen medicine Limited proteolysi Molecule Animals Trypsin Molecular Biology Mass spectrometry Chemistry Mass spectrometric Peptide Fragments Domain swapping Cattle Dimerization medicine.drug Research Article |
| Zdroj: | Scopus-Elsevier |
| Popis: | Dimeric seminal RNase (BS-RNase) is an equilibrium mixture of conformationally different quaternary structures, one characterized by the interchange between subunits of their N-terminal ends (the MXM form); the other with no interchange (the M=M form). Controlled tryptic digestion of each isolated quaternary form generates, as limit digest products, folded and enzymatically active molecules, very resistant to further tryptic degradation. Electrospray mass spectrometric analyses and N-terminal sequence determinations indicate that trypsin can discriminate between the conformationally different quaternary structures of seminal RNase, and exerts a differential and asymmetric action on the two dimeric forms, depending on the original quaternary conformation of each form. The two digestion products from the MXM and the M=M dimeric forms have different structures, which are reminiscent of the original quaternary conformation of the dimers: one with interchange, the other with no interchange, of the N-terminal ends. The surprising resistance of these tryptic products to further tryptic action is explained by the persistence in each digestion product of the original intersubunit interface. |
| Databáze: | OpenAIRE |
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