Erythrocytic diagnostic agents for determining antibodies to Proteus O antigens

Highly sensitive and specific erythrocyte diagnostic agents (ED) for the determination of antibodies to Proteus O-antigens have been obtained by the sensitization of formolated sheep red blood cells (SPBC) with activated lipopolysaccharides (LPS) without the use of mediators. The tannin treatment of formolated SRBC and/or the increase of temperature from 45 degrees C to 100 degrees C in the process of the preparation of ED have been found to produce no increase in effectiveness. Antibody ED permitting the detection of Proteus O- and H-antigens has been obtained by the sensitization of formolated chick red blood cells with immunoglobulin preparations to Proteus hydroxylamine antigens, carried out with the use of amidol. The experiments have shown the possibility of using this antibody ED for the determination of O-antibodies in the antigen neutralization test with nonactivated LPS used as an agglutinating agent. The passive hemagglutination test with antibody ED has proved to be a more sensitive method for the detection of O-antibodies than the antigen neutralization test with antigenic ED. The determination of Proteus etiology in the passive hemagglutination test with the use of antigenic ED has been shown to be highly effective in the examination of patients with chronic osteomyelitis at the stage of exacerbation.     

Selective electric-current inhibition of signals from the C fibers in nerve fiber microbundles: a method for identifying A and C afferents

Direct electric current of 3 microA applied through platinum electrode during 10 s to a fine strand teased mechanically from saphenous nerve, inhibits selectively C-fibre spikes in the strand and does not inhibit A-fiber spikes. The selective inhibition of C-fibers spikes in a fine strand is proposed as a method to identify a type of a single nerve fiber.     

Phenylalanine hydroxylase of human embryos: its homology with the enzyme from the liver of adults

Phenylalanine hydroxylase (PH) activity was discovered in the liver of 7-12 week old human embryos. Embryonic and adult PHs were identical, as shown by immunoelectrophoresis. Unlike the adult liver PH, the PH content of the extract of cytoplasmic proteins of embryonic liver was reduced but the specific activity was increased more than by one order of magnitude. H (57,000 D) and L (55,000 D) subunits were detected by immunoblotting. The L subunit predominates in the extract of membrane proteins of embryonic liver. Hence, the major part of phenylalanine oxidizing activity in the embryonic liver is related to the enzyme immunochemically identical with the PH of adult liver but differing from it in some structural and functional properties.     

Immunoperoxidase localization of fibronectin during odontoblast differentiation. An ultrastructural study

Immunoperoxidase labeling of fibronectin in one-day-old mouse first lower molars allowed to visualize a striking redistribution of this glycoprotein during terminal cytodifferentiation of odontoblasts. The modifications involved both extracellular and cell surface localizations. The possible roles of these modifications in terminal differentiation of odontoblasts are discussed.     

Method of isolating conditionally-pathogenic Gram-negative microorganisms, agents of intrahospital infections, from air

The possibility of detecting Pseudomonas aeruginosa and other Gram-negative bacteria in the air of the burn department at the Institute of Surgery was studied. The investigation of large volumes of air (0.5-1 m3) in the wards and the corridor with the use of a new bacteriological aerosol sampler, model IIAB-5, resulted in the detection of Pseudomonas aeruginosa. Besides, in a number of other rooms Klebsiella, Proteus, Citrobacter and Enterobacter were detected in the air. The possibility of the spread of Gram-negative opportunistic bacteria through the air in hospital conditions is discussed.     

Starch Binding Domain-containing Protein 1/Genethonin 1 Is a Novel Participant in Glycogen Metabolism

Stbd1 is a protein of previously unknown function that is most prevalent in liver and muscle, the major sites for storage of the energy reserve glycogen. The protein is predicted to contain a hydrophobic N terminus and a C-terminal CBM20 glycan binding domain. Here, we show that Stbd1 binds to glycogen in vitro and that endogenous Stbd1 locates to perinuclear compartments in cultured mouse FL83B or Rat1 cells. When overexpressed in COSM9 cells, Stbd1 concentrated at enlarged perinuclear structures, co-localized with glycogen, the late endosomal/lysosomal marker LAMP1 and the autophagy protein GABARAPL1. Mutant Stbd1 lacking the N-terminal hydrophobic segment had a diffuse distribution throughout the cell. Point mutations in the CBM20 domain did not change the perinuclear localization of Stbd1, but glycogen was no longer concentrated in this compartment. Stable overexpression of glycogen synthase in Rat1WT4 cells resulted in accumulation of glycogen as massive perinuclear deposits, where a large fraction of the detectable Stbd1 co-localized. Starvation of Rat1WT4 cells for glucose resulted in dissipation of the massive glycogen stores into numerous and much smaller glycogen deposits that retained Stbd1. In vitro, in cells, and in animal models, Stbd1 consistently tracked with glycogen. We conclude that Stbd1 is involved in glycogen metabolism by binding to glycogen and anchoring it to membranes, thereby affecting its cellular localization and its intracellular trafficking to lysosomes.