ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Untersuchungen über die Enzyme von Bläuepilzen (1969)
    Springer
    Archives of microbiology 67 (1969), S. 28-50 
    Details
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Zusammenfassung Drei Bläuepilze wurden in einer ungepufferten Nährlösung mit Glucose bzw. Carboxymethylcellulose (CMC) als Kohlenstoffquelle kultiviert. Die Kulturflüssigkeit wurde als Rohfermentlösung für den Nachweis von Cellulase (Carboxymethylcellulase), Polygalakturonase, Pektinesterase und p-Diphenol-oxidase benutzt. 1. Jeder der Versuchspilze schied die vier gepr\:uften Enzyme aus. 2. Die Enzymproduktion wurde durch den pH-Wert der N\:ahrl\:osung beeinflu\sBt. F\:ur die Polygalakturonase von Alternaria ergab sich hierbei eine auffallende Empfindlichkeit gegen\:uber pH-Werten um den Neutralpunkt. 3. Bei Aureobasidium deuten der Verlauf der pH-Optimumkurve sowie die Stabilit\:at des pektinolytischen Enzyms in neutraler N\:ahrl\:osung auf die Wirkung einer Polygalakturonid-Lyase hin. Mit Unterstützung durch die Deutsche Forschungsgemeinschaft. 4. Mit Glucose als C-Quelle stieg zu Beginn des Pilzwachstums die Acidit\:at an, w\:ahrend mit CMC in der N\:ahrl\:osung sich die pH-Werte sogleich zum Neutralpunkt verschoben. 5. In der Glucose-L\:osung war die Produktion der Cellulasen erheblich st\:arker als in der N\:arhl\:osung mit CMC. 6. Zur Ermittlung optimaler Versuchsbedingungen wurden f\:ur Cellulasen und Polygalakturonasen einige Enzymeigenschaften untersucht.
    Notes: Summary Three blue-stain fungi were cultivated in an unbuffered nutrient solution with glucose or carboxymethyl cellulose (CMC) as carbon source. The culture filtrates were used for detecting cellulase (carboxymethyl cellulase), polygalacturonase, pectinesterase and p-diphenoloxidase. 1. Each of the fungi produced these four enzymes. 2. The production of the enzymes was influenced by the pH value of the medium. The polygalacturonase of Alternaria showed a remarkable sensibility to pH values about 7. 3. For Aureobasidium the course of the pH optimum curve as well as the stability of the pectic enzyme in neutral solution suggest the presence of a polygalacturonide lyase. 4. With glucose as carbon source the acidity increased at the beginning of the fungal growth, whereas with CMC the pH values changed immediately to the neutral point. 5. In the glucose solution the production of cellulase was higher than in the medium with CMC. 6. To find most favorable experimental conditions some properties of cellulases and polygalacturonases were investigated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00413679
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Untersuchungen über die Enzyme von Bläuepilzen (1971)
    Springer
    Archives of microbiology 79 (1971), S. 140-146 
    Details
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Zusammenfassung 1. Der Bläuepilz Aureobasidium pullulans synthetisiert eine Pectintranseliminase (PTE) und eine Mannanase. 2. Die PTE hat ein pH-Optimum um 6,5 und wirkt nur mit Pectin als Substrat. 3. Das hydrolytisch wirkende Enzym (Pectinase bzw. Polygalakturonase) vermag sowohl Pectin als auch Polygalakturonsäure (PGS) abzubauen. Mit PGS liegt der optimale pH-Wert dieses Enzyms bei pH 4,5. 4. Mannanase ist am aktivsten um pH 4; die Enzymaktivität wird durch das Viscositätsverhalten von Polygalaktomannan bei verschiedenen Substratkonzentrationen beeinflußt.
    Notes: Summary 1. The blue-stain fungus Aureobasidium pullulans produces a pectin trans-eliminase (PTE) and a mannanase. 2. The PTE has a pH optimum at 6.5 and splits only pectin. 3. The hydrolytic enzyme (pectinase resp. polygalacturonase) degrades pectin as well as polygalacturonic acid (PGS). With PGS this enzyme shows its maximum activity at pH 4.5. 4. The greatest activity of mannase was found at pH 4; the enzyme activity is influenced by the viscosial behaviour of polygalactomannan at different substrate concentrations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00424921
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Molecular hydrogen: A new inhibitor of photosynthesis in the blue-green alga (cyanobacterium), Anabaena sp. TA 1 (1980)
    Springer
    Archives of microbiology 126 (1980), S. 1-10 
    Details
    ISSN: 1432-072X
    Keywords: Anabaena sp. ; Nitrogenase ; H2-inhibition ; Photosynthesis ; Pigment concentration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Molecular hydrogen strongly inhibits C2H2-reducing activity in intact cells of Anabaena sp. TA 1 in the light under anaerobic conditions. The inhibitory effect can be partially relieved by supplying the cells with molecular oxygen. When cells of Anabaena sp. TA 1 were grown under anaerobic N2-fixation conditions in the presence of 0.05 bar H2 with white light a pronounced decrease of growth rate occurred. With ammonium ions as nitrogen source the inhibitory effect of H2 was less pronounced. Concomitant with the reduced growth under N2 in the presence of H2 a loss of blue-green pigmentation was observed due to a diminished phycocyanin content. On the other hand, the concentration of carotenoids and chlorophyll remained nearly constant. With NH 4 + as nitrogen source nearly no alteration of phycocyanin content occurred upon incubation with H2. In addition, H2 induced a random distribution of thylakoid membranes in vegetative cells which normally exhibited a curved, parallel pattern. In heterocysts, however, photosynthetic membranes were always arranged randomly. Under far red light, growth and activity of photosystem II were largely diminshed. Under these conditions H2 exhibits an additional inhibitory effect. However, compared to 62% growth inhibition under white light, a decrease of only 20% occurred. Measurements of the photosynthetic electron flow with isolated thylakoid membranes showed that oxidation of diphenylcarbazide (DCP) by membranes from H2-grown cells was inhibited by 28% compared to membranes from control cells. Using ascorbate/DCPIP as electron donor an inhibition of only 1–4% was measured. It is concluded, that H2 inhibits electron flow in the photosynthetic electron transport chain at a site between photosystem II and photosystem I.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00421884
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Kinetics and properties of β-ketothiolase from Clostridium pasteurianum (1975)
    Springer
    Archives of microbiology 103 (1975), S. 21-30 
    Details
    ISSN: 1432-072X
    Keywords: β-Ketothiolase ; Clostridium pasteurianum ; Alcaligenes eutrophus H 16 ; Isoenzymes ; Inhibition/Inactivation by Coenzyme A
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. Ketothiolase of Clostridium pasteurianum was purified 130-fold by ammonium sulphate fractionation and by column chromatography using DEAE-Sephadex A-50 and hydroxylapatite. Subjected to gel electrophoresis β-ketothiolase revealed two distinct bands; by isoelectric focusing two enzymes with isoelectric points at pH 4.5 and 7.6 were separated. As established by sucrose density gradient centrifugation the molecular weight of both enzymes was found to be 158000. 2. The condensation reaction was measured by a coupled optical test using β-hydroxybutyryl-CoA dehydrogenase as auxiliary enzyme and either acetyl-CoA or free coenzyme A plus acetyl-phosphate and phosphotransacetylase (regenerating system) or acetyl-CoA plus regenerating system as substrates. β-Ketothiolase from C. pasteurianum used only 20% of the chemically synthesized acetyl-CoA; the enzyme from Alcaligenes eutrophus H 16 used 25%. When the regenerating system was added the condensation reaction continued. The enzyme from C. pasteurianum was inactivated by free coenzyme A, while the enzyme from A. eutrophus was inhibited. When acetyl-CoA was added as the substrate the initial velocity determination was impeded by the lack of linearity. With acetyl-CoA as the substrate the K m -value was found to be 2.5 mM acetyl-CoA. If free CoASH (or acetyl-CoA) plus regenerating system was added the K m was 0.44 mM (0.42 mM) acetyl-CoA. 3. The β-ketothiolase activity was measured in the direction of acetoacetyl-CoA cleavage by an optical assay following the decrease of the enol and chelate form of acetoacetyl-CoA by absorption measurement at 305 nm. The activity was maximal at 24 mM MgCl2. The apparent K m values for acetoacetyl-CoA were 0.133 mM and 0.105 mM with 0.065 and 0.016 mM CoASH, respectively. The K m -values as calculated for only the keto form of acetoacetyl-CoA were 0.0471 and 0.0372 mM, respectively. The cleavage reaction was inhibited by high acetoacetyl-CoA concentrations; the inhibition was partially relieved by CoASH. In the range of low concentrations of acetoacetyl-CoA only a slight inhibition by CoASH was observed. The K m for CoASH was found to be 0.0288 and 0.0189 mM with 0.09 and 0.045 mM acetoacetyl-CoA, respectively. High concentrations of CoASH exerted an inhibitory effect on the cleavage reaction. With respect to enzyme kinetics and sensitivity to inhibitors and metabolites the β-ketothiolases of C. pasteurianum and A. eutrophus were rather similar.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00436325
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Identification and physiological characterization of the nitrogen fixing bacterium Corynebacterium autotrophicum GZ 29 (1976)
    Springer
    Archives of microbiology 108 (1976), S. 17-26 
    Details
    ISSN: 1432-072X
    Keywords: Nitrogen fixation ; Aerobic hydrogen bacteria ; Oxygen sensitivity ; Efficiency ; Aerobic and anaerobic acetylene reduction ; Corynebacterium autotrophicum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The coryneform hydrogen bacterium strain GZ 29, assigned to Corynebacterium autotrophicum fixed molecular nitrogen under autotrophic (H2, CO2) as well as under heterotrophic (sucrose) conditions. Physiological parameters of nitrogen fixation were measured under heterotrophic conditions. The optimal dissolved oxygen concentration for cells grown in a fermenter with N2 was rather low (0.14 mg O2/l) compared with cells grown in the presence of NH 4 + (4.45 mg O2/l). C. autotrophicum GZ 29 had a doubling time of 3.7 h at 30°C with N2 as N-source and sucrose as carbon source and at optimal pO2. Acetylene reduction reached values of 12 nmoles of ethylene produced/minxmg protein. Although the oxygen concentration in the growing culture was kept constant, the optimal dissolved oxygen tension for the acetylene reduction assay shifted to higher pO2-values. The overall efficiency of nitrogen fixation amounted to 22 mg N fixed/g sucrose consumed; it reached a maximal value of 65 mg N fixed/g sucrose consumed at the beginning of the exponential growth phase. Intact cells reduced acetylene even under anaerobic test conditions; further anaerobic metabolic activity could not be ascertained so far.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425088
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Activity of the H2-oxidizing hydrogenase in different N2-fixing bacteria (1979)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 6 (1979), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1979.tb04305.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Interacting mechanisms of organic sulfides with metallic surfaces and their importance for problems of friction and lubrication
    Amsterdam : Elsevier
    Applications of Surface Science 4 (1980), S. 154-161 
    Details
    ISSN: 0378-5963
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0378-5963(80)90124-5
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Atomabsorptions-spektrometrische bestimmung kleiner substanzmengen und analyse von Spurenkonzentrat-mit der Injektionsmethode
    Amsterdam : Elsevier
    Spectrochimica Acta Part B: Atomic Spectroscopy 30 (1975), S. 169-177 
    Details
    ISSN: 0584-8547
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0584-8547(75)80015-2
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Preconcentration of trace elements from pure manganese and manganese compounds with activated carbon as collector
    Amsterdam : Elsevier
    Analytica Chimica Acta 93 (1977), S. 45-52 
    Details
    ISSN: 0003-2670
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0003-2670(77)80005-6
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Improvement of the detection power in electrothermal atomic absorption spectrometry by summation of signals
    Amsterdam : Elsevier
    Analytica Chimica Acta 200 (1987), S. 573-579 
    Details
    ISSN: 0003-2670
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0003-2670(00)83802-7
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...