Cereal grain resorcinolic lipids inhibit H2O2-induced peroxidation of biological membranes.

Cereal grain resorcinolic lipids (5-n-alk(en)ylresorcinols) at micromolar concentrations are able to protect the erythrocyte membrane against hydrogen peroxide-induced lipid oxidation. The antioxidative effect is dependent upon chain length of alkylresorcinol molecules. The C15:0 homolog (IC50 of 10 microM) exhibited strongest activity whereas for long chain homologs (C19:0 and C23:0) IC50 values were higher, 32.5 and 59 microM, respectively. The protective effect of alkylresorcinolic antioxidants was also dependent on their incorporation into the membrane, that is governed by their water-membrane partition coefficient. The results obtained show that alkylresorcinols should be recognized as hydrophobic, membrane-localised antioxidants.

A randomised, double-blind study on the efficacy of Tolpa Torf Preparation (TTP) in the treatment of recurrent respiratory tract infections.

TTP is a new immunomodulating drug of natural origin, registered in Poland for human use. In the randomised, double blind study to assess the therapeutic efficacy of the Tolpa Torf Preparation (TTP) in the recurrent respiratory tract infectious participated 39 young patients (age 16-22). TTP was administered orally, 5 mg daily for three weeks. During 3 months follow-up period favourable results of treatment were obtained in 14 of 20 TTP treated patients and in 8 of 19 of the placebo patients. The therapeutic effects were seen even after the 6 months follow-up period. The phagocytic activity of granulocytes was significantly stimulated in the TTP--treated patients but not in the placebo-treated patients. The results suggest that TTP is effective drug in the treatment of recurrent respiratory tract infections with undefined infectious etiology. In the period of the treatment as well as during 6 months observation no side effects were noticed.

[Chlamydia-induced pneumonia in children]. / Die durch Chlamydien verursachte Lungenentzündung bei Kindern.

Three cases of pneumonia caused by Chlamydia were observed. The disease ran a protracted course and was refractory to treatment. Erythromycin was given initially intravenously and then orally, with improvement of the general condition of children and regression of inflammatory changes in the lungs. Such cases are worth of reporting in view of only isolated reports on respiratory infections caused by these organisms.

Protein inhibitors of trypsin from the seeds of Cucurbitaceae plants.

Seven trypsin inhibitors were isolated from the seeds of Cucurbitaceae plants: two from cucumber (Cucumis sativus) and red bryony (Bryonia diotica) and one from figleaf gourd (Cucurbita ficifolia), spaghetti squash (Cucurbita pepo var. (vegetable spaghetti) and water melon (Citrullus vulgaris). The inhibitors were purified by fractionation with ammonium sulphate, followed by ion-exchange chromatography and affinity chromatography using immobilized trypsin or anhydro-trypsin. The homogeneous inhibitors from cucumber and water melon are made up of 32 and 30 amino acid residues, respectively, whereas the remaining ones of 29 residues. All inhibitors contain three disulphide bridges and are free of threonine, phenylalanine and tryptophan. Inhibitors from spaghetti squash and CSTI IIb from cucumber are inactivated by acetylation of free amino groups whereas the remaining ones are inactivated by modification of arginine with 1,2-cyclohexanedione. Thus the P1 residues of the reactive sites of the inhibitors are lysine and arginine, respectively.

Isolation and partial amino acid sequence of the trypsin inhibitor from the seeds of Cucurbita maxima.

Trypsin inhibitor from squash (Cucurbita maxima) seed was extracted with 0.1 M-acetate buffer, pH 4.5, purified on immobilized trypsin, and separated by SE-Sephadex C-50 chromatography into three active fractions. All of them inhibited trypsin to the same extent, showed no antichymotrypsin or antikallikrein activity, had a similar molecular weight (about 3300), and contained no tryptophan, phenylalanine or threonine. The partial amino acid sequence of tryptic and peptic peptides of fraction III was determined by Edman degradation procedure.