ulczyk M

Bacteriophage Therapy of Bacterial Infections: An Update of our Institute’s Experience

1307 patients with suppurative bacterial infections caused by multidrug-resistant bacteria of different species were treated with specific bacteriophages (BP). BP therapy was highly effective; full recovery was noted in 1123 cases (85.9%). In 134 cases (10.9%) transient improvement was observed and only in 50 cases (3.8%) was BP treatment found to be ineffective. The results confirm the high effectiveness of BP therapy in combating bacterial infections which do not respond to treatment with the available antibiotics.

Bacteriophage therapy for infections in cancer patients

Abstract Cancer patients are known to be immunocompromised and susceptible to infections. We have used bacteriophages matched for specific bacterial isolates, to treat antibiotic-resistant infections in those patients. Cure of infection was achieved in all cases, indicating very high efficacy of bacteriophage therapy.

Chemical studies on the specific fragment of Shigella sonnei phase I

Abstract When a dry bacterial mass of Shigella sonnei phase I was extracted with phenol-water a specific lipopolysaccharide and cell ribonucleic acids were obtained as a water-soluble material. In order to obtain the specific fragment, the material was subjected to acid hydrolysis with 0.25 M H 2 SO 4 for 1 h at 100°. These conditions of hydrolysis proved to be optimal, i.e. maximal degradation and minimal loss of serological activity of the initial material was achieved. A procedure for the resolution of the specific fragment from other components, such as inactive oligo- and mono-saccharides of the lipopolysaccharide and products of hydrolysis of the ribonucleic acids, has been developed. The examination of the chemical composition of the specific fragment revealed its glycoprotein character. It contains the monosaccharides galactose, glucose, glucosamine and galactosamine, and the amino acids aspartic acid, glutamic acid, serine, glycine, alanine, threonine and lysine. The specific fragment does not exhibit protein character: it gives no Lowry or biuret reaction and is resistant to the action of pronase. The specific fragment is homogenous during ultracentrifugation and in free-solution electrophoresis. Its sedimentation coefficient is 1.46 S. During ultra-filtration it passes through a dialysis membrane.

Glycyl peptidase in human serum and tissues.

Since Gomori in 1954 described the enzymatic hydrolysis of glycyliuand -/3-naphthylamides [l] , many amino acid as well as peptide naphthylamides have been obtained and used as chromogenic substrates for peptidases. Later it was demonstrated that the naphthylamide substrates are not hydrolysed by known classical peptidases but by enzymes named arylamidases [2,3]. In this paper a calorimetric method for determination of glycyl peptidase activity using new Nglycyl-7-L-glutamyl+naphthyl amide is described. The enzyme was purified from human plasma and evidence is provided that it is different from that hydrolysing glycyl-&naphthylamide.