Changes of intraocular pressure in patients with open-angle glaucoma in relation to the passage of atmospheric fronts and environmental contamination

Effects of atmospheric frontal passages on intraocular pressure (IOP) in patients with open-angle glaucoma are statistically investigated to show the meteorotropism of this disease. Changes in IOP caused by frontal passages are evident; the response is not identical in all the patients near the day of the passage of a warm front, while on the third day following the passage of the front a well pronounced drop in IOP occurs. Anomalous increases of IOP over several months' duration occurred in the years 1986–7. This finding is explained in relation to the hypothesis of environmental contamination in Central Europe by radioactive cesium nuclides due to the Chernobyl accident.     

Fluorescence investigation of the sex steroid binding protein of rabbit serum: steroid binding and subunit dissociation

The relationship between steroid binding and protein subunit interactions of rabbit sex steroid binding protein (rSBP) has been studied by steady-state and time-resolved fluorescence spectroscopy. The high-affinity (Ka approximately 10(8) M-1 at 4 degrees C), fluorescent estrogen d-1,3,5(10),6,8-estrapentaene-3,17 beta-diol [dihydroequilenin (DHE)] was used as a fluorescent probe of the steroid-binding site. Perturbation of the binding site with guanidinium chloride (Gdm.Cl) was monitored by changes in the steady-state fluorescence anisotropy of DHE as well as by changes in fluorescence quenching of DHE with acrylamide. The results of acrylamide quenching at 11 degrees C show that, while between 0 and 1 M Gdm.Cl the steroid-binding site is completely shielded from bulk solvent, there is decreased DHE binding. To study the subunit-subunit interactions, rSBP was covalently labeled with dansyl chloride in the presence of saturating 5 alpha-dihydrotestosterone (DHT), which yielded a dansyl-conjugated protein that retained full steroid-binding activity. The protein subunit perturbation was monitored by changes in the steady-state fluorescence anisotropy of the dansyl group. At 11 degrees C, the dansyl anisotropy perturbation, reflecting changes in global and segmental motions of the dimer protein, occurs at concentrations of Gdm.Cl above 1 M. The Gdm.Cl titration in the presence of steroids with equilibrium association constants less than 10(8) M-1 shows a plateau near 3 M Gdm.Cl at 11 degrees C; at this Gdm.Cl concentration, no DHE is bound. No plateau is observed at 21 degrees C. At higher Gdm.Cl concentrations, the dansyl fluorescence anisotropy decreases further and shows no steroid dependence. Recovery of steroid-binding activity (assayed by saturation binding with [3H]DHT), under renaturation conditions, is dependent on both steroid concentration and affinity. Both unlabeled and dansyl-labeled protein recovery the same amount of activity, and according to fluorescence anisotropy, dansyl-labeled rSBP re-forms a dimer upon dilution below 1 M or removal of Gdm.Cl. From the steroid requirement for recovery of steroid-binding activity, it appears that a conformational template is required for the dimeric protein to re-form a steroid-binding site with native-like properties.     

Catabolite repression of different inducible enzymes inEscherichia coli and the effect of cAMP

Simultaneous induction of two enzymes sensitive to catabolite repression does not lead to an additive decrease of the specific activity of the two. Exogenously added cAMP increases the specific activity of catabolically repressed enzymes, irrespective of whether the enzyme is induced separately or simultaneously with another enzyme. In the presence of 12 different substrates metabolized by inducible enzymes glucose does not bring about catabolite repression. Synthesis of cAMP is identical with that occurring under conditions when glucose brings about catabolite repression.     

The mechanism of resistance to streptomycin inEscherichia coli. Functional analysis of the permeability barrier of cells harbouring the Rldrd-19Km plasmid

The mechanism of phenotypically altered SM resistance in mutants of Escherichia coli JC5455 (Rldrd-19Km-) lrs and JC5455 (pON5300) was compared with that of the standard strain JC5455 (Rldrd-19Km-). On analyzing the membrane polypeptides in polyacrylamide gel both mutants were found to possess a protein spectrum different from that of ths standard strain. Transport of D-xylose and L-arginine was the same in all strains, transport of L-proline was decreased in JC5455 (pON5300) which may indicate a mutational interference with energy metabolism. The basic uptake of dihydrostreptomycin was the same in all strains but there were differences after preincubation of cells with streptomycin or glucose. The increased resistance of JC5455 (Rldrd-19Km-) lrs may be due to observed quantitative differences in membrane polypeptides that might play a role in the binding and functional expression of aminoglycoside-3'adenylyl transferase which modifies streptomycin. The increased sensitivity toward streptomycin in JC5455 (pON5300) can be explained by a mutation due to N-methyl-N'-nitro-N-nitrosoguanidine in the host cell since this change of sensitivity to streptomycin could not be transferred by transformation into a nonmutagenized strain. The coincidence of inducibility of increased transport of streptomycin by this antibiotic and the altered frequency of reversion to high levels of streptomycin resistance in JC5455 (pON5300) and in the transformant JC5455 (pON5302) may indicate that the altered reversibility toward phenotypically high resistance to streptomycin is a property of pON5300 and is transferred by transformation.     

Transport properties of two extremely thermophilic species ofThermus

Thermus flavus and T. ruber grew optimally at 75 and 60 °C, respectively, but transport of monosaccharides (D-quinovose) and ammo acids (2-aminoisobutyric acid) had optima about 20 °C lower. Both transports were active, inhibited by 2,4-dinitrophenol but hardly at all by uranyl(2+) ions. Several transport systems are apparently involved with each class of compounds. Preincubation with glucose curtailed subsequent transport severely. Practical cessation of transport below 35 °C may be associated with the rather uniform composition of membrane lipids where iso- and anteiso-C₁₅ and C₁₇ acids are practically the only components.     

Microorganisms in the rhizosphere of wheat colonized by the fungusGaeumannomyces graminis var.tritici

The population of microorganisms in wheat rhizosphere changed in the presence of the fungus Gaeumannomyces graminis var. tritici causing the take-all of wheat. In the majority of cases when the soil was artificially contaminated by the fungus, both the number of bacteria in the rhizosphere and the bacteria/fungi ratio temporarily increased. At the beginning bacteria growing in the presence of NH4+ predominated, later bacteria utilizing organic N-substances prevailed. Pseudomonas fluorescens and the related species colonized the rhizosphere and the soil to a greater extent in the presence of G. graminis. The wheat rhizosphere with G. graminis was found to contain a higher level of the slime-producing bacterium Agrobacterium spp.; this microorganism occurred on hyphal surfaces (in hyphosphere) of both G. graminis growing in soil and Mucor spp. Changes in microbial populations in the wheat rhizosphere during the first stage of colonization by G. graminis can be partly explained by a simultaneous rhizosphere colonization by microorganisms which accompany this fungus in soil. In the period of increase in the number of bacteria in rhizosphere a temporary stimulation of wheat growth was observed.     

Reversion of anomalous forms ofBacillus subtilis

Anomalous forms ofBacillus subtilis A 32 produced by prolonged cultivation in a chemostat under nitrogen limitation are described. A change in the cultivation conditions brings about a transformation of these forms to bacillar rods. The transformation is gradual and lasts for several generations.     

A contribution to the phenotype distribution of phosphoglucomutase in Czechoslovakia (the district of České Budějovice)

Summary A population sample of 416 unrelated donors from eské Budjovice (southorn Bohemia) was investigated for the phenotypes of phosphoglucomutase (PGM). The calculated frequencies of the allelles PGM ₁ ¹ and PGM ₁ ² , 0.770 and 0.230, respectively, correspond to the expected frequencies of the phenotypes PGM 1=0.593, PGM 2-1=0.354, and PGM 2=0.0529. No rare phonotype was detected.