[Isolation of inactive phenylalanine hydroxylase from autopsy specimens of human liver]. / Poluchenie neaktivnogo belka fenilalaningidroksilazy iz autoptatov pecheni cheloveka.

An electrophoretically homogeneous protein has been isolated from human liver autoptats, using a procedure employed for the isolation of phenylalanine hydroxylase from rat liver. The procedure includes chromatography of liver extracts on phenyl-Sepharose and subsequent purification on DEAE-Toyopearl. The activity of phenylalanine hydroxylase in the autoptats was markedly decreased in comparison with that in bioptats. The isolated protein possessed no enzymatic activity. However, the subunit composition of the protein, the molecular masses of protein subunits (55 and 57 kD) and the amino acid composition were close to those of the human enzyme. Antibodies to the protein inhibited the phenylalanine hydroxylase activity in human liver bioptats and weakly inhibited the rat enzyme. The experimental results suggest that the structural organization of phenylalanine hydroxylase does not alter as a result of the loss of enzymatic activity in cadaverous human liver.

[Role of a microbial factor, necrotic tissue and a foreign body in the development of wound suppuration]. / Rol' mikrobnogo faktora, nekroticheskikh mass i inorodnogo tela v razvitii gnoinogo protsessa v ranakh.

The effect of microorganisms, necrotic tissues and a foreign body on the development of festering process in rat wounds was studied. It was found that the presence of necrotic tissues is the necessary and sufficient condition for a clinical manifestation of infection in rat wounds. Additional infection of the wounds and introduction of a foreign body did not appreciably change the clinical picture. A model is suggested of a festering wound in rats without artificial infecting. In the festering wound, one could observe the replacement of the gram-positive coccal microflora by the gram-negative one. Meanwhile the gram-positive coccal microflora was predominant in the non-festering wound. The level of potential biochemical indicators of infection in the blood of animals with festering wounds was higher than in the blood of those with non-festering wounds. The morphology, and the content of microbial cells, the content of nucleic acids, and total proteolytic activity in festering wound tissues were examined over time.

[Comparative biochemical study of 2 natural inactive variants of the actinomycin C producer Actinomyces sp. 26-115 with varying sensitivity to actinomycin]. / Sravnitel'noe biokhimicheskoe izuchenie dvukh estestvennykh neaktivnykh variantov produtsenta aktinomitsina C Actinomyces sp. 26-115 s razlichnoi chuvstvitel'nost'iu k aktinomitsinu.

Two natural variants of the actinomycin C-producing organism Actinomyces sp-26-115, i.e. H1 and H2 differ in their sensitivity to exogenic actinomycin, colony morphology, growth dynamics on the synthetic medium and stability to ultrasound and lysozyme. Both variants synthesize no actinomycin. Variant H1 is sensitive to exogenic actinomycin, while variant H2 is resistant to it. Variants H1 and H2 have some similarity in the composition of membrane proteins. Still, they differ in the protein molecular masses, which are equal to 600000--500000, 220000, 130000. The active variant A and nonactive variant H2 have the most similar compositions of membrane proteins. These variants are also close in their growth dynamics, colony morphology, sensitivity to ultrasound and lysozyme. The membranes of all the variants studied contain phosphatidyl ethanol amide as the main phospholipid component. Insignificant differences are observed only with respect to the minor components. The content of teichoic acids in the cell walls of variant H2 is very high, slightly changes during the developmental stage and insignificantly increases on addition of actinomycin to the medium. The cell wall of variant H1 contains less amounts of teichoic acids. During the developmental stage they are liberated from the wall at a higher rate than peptidoglycan. The sensitivity to actinomycin does not increase with an increase in the culture age. It is probable that teichoic acid of the cell wall is one of the factors providing resistance to actinomycin in variant H2. It may be considered as a barrier preventing transport of exogenic actinomycin into the cell.