Yeast invertase: Subcellular distribution and possible relationship between the isoenzymes

The intracellular invertase ofSaccharomyces cerevisiae is mainly found in a soluble form (91–95%), while only minor amounts are found bound to the internal (4–8%) and plasma membranes (less than 1%). In the processes of derepression or repression, inhibition of RNA or protein synthesis, or in the presence of 2-deoxy-d-glucose, the levels of the membrane-bound and external activities are modified in a way in which their relation is clear, while the soluble enzyme does not change at all. These results, together with the fact that the membrane-bound and the external enzymes are glycoproteins, suggest a precursor-product relationship between the enzymic forms.     

Improved localization of thiamine pyrophosphatase activity in mounted cryostat sections using gel fixation and gel incubation media

Summary The presence of 1% agar in the fixation and substrate solutions for the histochemical demonstration of thiamine pyrophosphatase (4.4 mM TPP; 3.6 mM Pb²⁺; 0.025 Tris-maleate buffer, pH 7.2) clearly facilitates the localization of the enzyme in Golgi apparatus in cold microtome sections prepared from unfixed specimens.     

Cytotaxonomic study ofTragopogon L. in czechoslovakia

Karyotypes ofTragopogon orientalis L. subsp.orientalis, T orientalis L. subsp.leiocarpos (Sauter)Trnka,T. pratensis L.,T. minor Miller,T. dubius Scop. subsp.dubius andT. dubius Scop. subsp.major (Jacq.)Vollmann were studied. The occurrence in Slovakia ofT. pratensis was karyologically proved.     

Pleurotrema epiphylla Vězda sp. n., eine neue foliikole Flechte aus Zentral-Afrika

Eine nèue foliikole Flechte (Pleurotrema epiphylla sp. n.) aus Zaïre (Zentral-Afrika) wird beschrieben. Die systematischen Beziehungen der neuen Art zu den anderenPleurotrema-Arten und die Stellung der GattungPleurotrema innerhalb der FamilieParatheliaceae wird kurz diskutiert.     

13C-NMR of double and triple bond carbon atoms of unsaturated fatty acid methyl esters

The carbon magnetic resonance spectra of many fatty acid methyl esters with cis and trans double bonds and triple bonds at various positions and in many different combinations have been investigated.The influence of the ester group on double and triple bonds in the fatty acid chain depends strongly on the positions of these bonds. For a given position the influence is constant, even if one or more other double or triple bonds are present.Together with the evaluated chemical shift parameters for the effects of double and triple bonds on each other, complete assignments are possible and spectra of various types of unsaturated esters can be predicted with high accuracy (±0.1 ppm).     

Relationship between the structure of carbonylcyanide phenylhydrazones and inhibition of growth of microorganisms,stimulation of respiration of yeast cells and rat liver mitochondria

The effect of ten derivatives of carbonylcyanide phenylhydrazone on growth of bacteria, yeast and different species of filamentous fungi was investigated. In yeast and mitochondria isolated from rat liver the effect of these derivatives on the respiratory activity was also followed. The relative efficiency of the individual derivatives of earbonylcyanide phenylhydrazone was determined on the basis of the results obtained. It was shown that derivatives, in which the substituent on the benzene ring causes simultaneously an increase of acidity and lipophilicity of the derivative as compared with the non-substituted carbonylcyanide phenylhydrazone (4-trifluoromethoxy-, 3-chloro-, 4-chloro and 3,4-dichloroderivatives) were most effective.     

Separation and properties of α-mannosidase and mannanase from the basidiomycetePhellinus abietis

Proteins of a crude enzyme preparation obtained from the cultivation medium of the basidiomycetePhellinus abietis were separated by gel filtration and ion-exchange chromatography. The preparation contained a minimum of three enzymes capable of splitting α-d-mannosidic bonds: α-mannosidase, exomannanase, and endomannanase, which were separated. Some properties of the mannanase complex of the crude enzyme preparation, and of a partially purified α-mannosidase were examined. The mannanase complex exhibited two pH optima, its temperature optimum being at 46 °C The pH optimum of purified α-mannosidase was at pH 5.0, the temperature optimum was at 60 °C; the enzyme had a relatively high heat stability. The K_m of α-mannosidase forp-nitrophenyl α-d-mannopyranoside was 1.5 x 10⁻⁵ M. Pure α-mannosidase did not split mannan.