[Multi-stage anatomical-functional reconstruction in surgical treatment of cancer of the mouth floor and tongue]. / Wieloetapowa anatomiczno-czynnosciowa rekonstrukcja w leczeniu chirurgicznym raka dna jamy ustnej i jezyka.

Authors present multistage surgical treatment of cancer disease with its radical dissection and anatomical reconstruction of risected tissue diminution and consecutive functional reconstruction of organs and tissue elements in later stage.

[On diagnosis and treatment of parotid tumors]. / W sprawie diagnostyki i leczenia guzów slinianki przyusznej.

The authors showed diagnosis and treatment of parotid tumours.

Comparison of conformational properties of proline and threonine residues.

The conformational role of Thr was investigated by 13C-n.m.r. and CD methods using a following series of tetrapeptides: Thr-Ala-Ala-Ala, Ala-Thr-Ala-Ala, Ala-Ala-Thr-Ala and Ala-Ala-Ala-Thr. It was found that introduction of Thr in every position of the tetraalanine peptide chain distinctly influences conformational equilibria of the peptides. An increase of beta-turn forms in conformational equilibria is induced by ionization of the terminal carboxyl group, independent of threonine position in the peptide chain. Threonine in position 1 or 3 of the peptide chain seems to have some importance for beta-turn formation in acid solution.

1H NMR spectra of trypsin inhibitors from seeds of Cucurbitaceae plants. Resonance signals of methyl groups.

1H NMR spectra (250 MHz) of four trypsin inhibitors isolated from seeds of Cucurbitaceae plants were studied. It was found that structural differences between the inhibitors from the genus Cucurbita and from the genus Cucumis consist, among others, in the presence in the former group of a valine residue strongly shielded from the solvent.

Structural differences between trypsin-inhibitors isolated from Cucurbitaceae family seeds: immunological, NMR and CD studies.

By manifold immunizations of rabbits with virgin or modified trypsin inhibitor III from squash seeds and trypsin inhibitor II b from cucumber seeds, specific antibodies were produced. In double immunodiffusion the anti-squash inhibitor antibody also gave weak precipitate arcs with inhibitor I from squash, inhibitor II from summer squash and with inhibitor I from zucchini, but not with inhibitor II b from cucumber seeds. The genus of Cucurbita trypsin inhibitors, preincubated with the antibody, lost their antitrypsin activity. The antibody showed a significantly weaker effect on the activity of the inhibitor from cucumber sees. 1H-NMR and CD spectra also confirm structural differences between trypsin inhibitors from the genus of Cucurbita and the cucumber (genus of Cucumis) inhibitor.

Conformation of model, alanine and proline containing tetrapeptides in water. Comparison of 13C-n.m.r. and CD results.

CD spectra of model alanine and prolyl-alanine tetrapeptides were measured at different pH values. An analysis of the spectra shows that proline in position 2 or 4 of a tetrapeptide favours folding of the peptide chain, and unfolding when it is in position 3. Changes in CD spectra evidence growing amounts of the beta-turn conformation upon increasing pH, independent of proline position in the peptide chain.

Steric effect exerted by the proline residue on the antecedent alanine residue.

Five model tetrapeptides: Ala-Ala-Ala-Ala, Pro-Ala-Ala-Ala, Ala-Pro-Ala-Ala, Ala-Ala-Pro-Ala and Ala-Ala-Ala-Pro, were synthesized and measured in D2O by 13 C-n.m.r. spectroscopy. The spectra analysis led us to the conclusion that for each model (irrespective of pD) in conformational equilibrium, the predominant conformation is the one in which side methyl of alanine preceding proline residue eclipses alanine carbonyl group. The influence of pD changes in cis-trans isomerism of Ala-Pro amide bond was also investigated.