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Protein Science, Vol 7, Issue 12 2653-2658, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Selective and asymmetric action of trypsin on the dimeric forms of seminal RNase

C. DE-LORENZO, F. D. PIAZ, R. PICCOLI, A. D. MARO, P. PUCCI and G. D'ALESSIO
Dipartimento di Chimica Organica e Biologica, Universita di Napoli Federico II, Via Mezzocannone 16, 80134 Naples, Italy

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.
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