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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 153 (1989), S. 7-11 
    ISSN: 1432-072X
    Keywords: Cyanobacterium ; Fischerella ; 3-Hydroxy fatty acids ; Lipopolysaccharide ; Outer membrane ; Sheath
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A purified sheath fraction and an outer membrane fraction were obtained from the cyanobacterium Fischerella sp. PCC 7414. The sheath had a fine structure with osmiophilic fibers running in parallel to the cell surface in two distinct layers. The sheath fraction contained mainly neutral sugars (Glc, Man, Gal, Xyl, Fuc, 2-O-methylhexose), GlcN, uronic acids, and minor components such as amino acids, sulfate, phosphate, and fatty acids. The protein moiety was removable from the sheath fraction by treatment with boiling sodium dodecyl sulfate. The presence of three different 3-hydroxy fatty acids (3-OH-14:0, 3-OH-16:0, 3-OH-18:0) in addition to GlcN indicated the presence of lipopolysaccharide in the outer membrane. One major (Mr 50,000) and two minor (Mr 54,000 and 65,000) proteins were detected as constituents of the outer membrane.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 156 (1991), S. 312-318 
    ISSN: 1432-072X
    Keywords: Cell wall ; Cyanobacterium ; Gloeobacter violaceus ; Lipopolysaccharide ; Outer membrane protein ; Peptidoglycan-polysaccharide complex ; Sheath
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sheaths isolated from Gloeobacter violaceus were found to be composed of a major polysaccharide moiety (glucose, galactose, rhamnose, mannose, arabinose), a protein moiety, and negatively charged components (glucuronic acids, phosphate, sulfate). Outer membrane polypeptide patterns were dominated by two major peptidoglycan-associated proteins (Mr 62,000 and 53,000). Lipopolysaccharide constituents were glucosamine, 3-hydroxy fatty acids (3-OH-14:0, anteiso-3-OH-15:0, 3-OH-16:0, 3-OH-18:0), carbohydrates, and phosphate. A1γ-type peptidoglycan and non-peptidoglycan components (mannosamine, glucose, mannose, and glucosamine) indicated the presence of a peptidoglycan-polysaccharide complex in the cell walls of Gloeobacter violaceus.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-072X
    Keywords: Rhodobacter capsulatus ; Chemostat ; Energy supply ; Nitrogen levels ; C/N ratio ; Nitrogenase activities ; Nitrogenase expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rhodobacter capsulatus strain 37b4 was grown phototrophically in chemostat cultures with 2 mM of ammonium chloride and 30 mM of malate at a constant dilution rate of 0.075 h-1. When illumination was raised from 3000 to 30000 lx, steady state biomass levels as well as malate uptake increased linearly with increasing illumination. Yet, in no case external ammonium could be detected in the culture fluid. Specific nitrogenase activity increased by a factor of ten between 3000 and 15000 lx and approached constancy above 15 000 lx. When samples were anaerobically withdrawn from the chemostat and subsequently grown in batch cultures under saturating light conditions, biomass increased to a constant level, independently of the illumination used in the previous chemostat culture. In fact, the specific nitrogen contents of cells were 0.195 and 0.154 (g of N per g of protein) with chemostat cultures adapted to 3000 and 30000 lx, respectively. With the former cultures, specific nitrogen contents decreased to 0.142 g of nitrogen per g of cell protein upon incubation in a batch system. This suggests the existence of free nitrogen compounds in cells of chemostat cultures, the concentrations of which decrease while protein levels increase with increasing energy supply. Intracellular amino acid pools revealed slightly elevated levels of major amino acids in low-light cultures as compared to high-light cultures. On the basis of intracellular levels of ammonium, however, no significant differences could be detected. Since, in addition, malate consumption increased linearly with increasing illumination, it is proposed that light controls nitrogenase in Rhodobacter capsulatus via the C/N ratio, as represented by malate and ammonium consumption, rather than directly.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-072X
    Keywords: Cyanobacteria ; Outer membrane ; Peptidoglycan ; associated protein ; Pore-forming protein ; Porin ; Synechococcus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pore-forming protein (porin) was isolated from N,N-dimethyl-dodecylaminoxid (LDAO)-extracted outer membranes of Synechococcus PCC 6301 and purified by ion exchange chromatography on DEAE-Sephacel column. The apparent molecular mass on SDS-PAGE was determined to be about 52000. The native porin was reconstituted into black lipid bilayer membranes and showed a single-channel conductance of 5.5 nS in 1 M KCl. The porin was found to be N-terminally blocked. The C-terminal amino acid sequence was identified as Phe-Thr-Phe. Amino acid analysis suggested that the porin protein consists of about 420 amino acid residues, yielding a polarity of 43.6% and a molecular mass of 45000 in contrast to the mobility on SDS-PAGE.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 142 (1985), S. 168-174 
    ISSN: 1432-072X
    Keywords: Carotenoids ; Cell wall ; Cyanobacterium ; Peptidoglycan-associated proteins ; Polypeptide pattern ; Synechocystis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cell walls free of cytoplasmic- and thylakoid membranes were isolated from Synechocystis PCC 6714 by sucrose density gradient centrifugation and extraction with Triton X-100. The Triton-insoluble cell wall fraction retained the multilayered fine structure. Peptidoglycan, proteins, polysaccharides, lipopolysaccharides, lipids and carotenoids were found as constituents of the cell wall. Polypeptide and lipid patterns of cell walls were completely different from that of the cytoplasmic/thylakoid membrane fraction. The purified cell walls contained about twelve outer membrane proteins. The two major polypeptides (Mr 67,000 and 61,000) were found to be associated with the peptidoglycan by ionic interactions. Myxoxanthophyll (major carotenoid), related carotenoid-glycosides and zeaxanthin were the predominating carotenoids of the cell wall of Synechocystis PCC 6714 over echinenone and β-carotene. A polar unknown carotenoid was observed, the absorption spectrum of which resembled that of myxoxanthophyll. It was exclusively found in cell walls, but not in the cytoplasmic/thylakoid membrane fraction.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-072X
    Keywords: Cell inclusions ; Cell wall ; Cytoplasmic membrane ; Freeze-fracture electron microsopy ; Gas vesicles ; Outer membrane ; Prochlorophyta ; Prochlorothrix hollandica ; Thylakoid membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The outer membrane of Prochlorothrix hollandica is covered with a network of fine fibrils on its surface and separated from the cytoplasmic membrane by an electrondense peptidoglycan layer (8 to 20 nm thick). The thylakoid membranes are arranged in stacked and unstacked regions which present four characteristic fracture faces with different numbers and sizes of intramembrane particles. Cell inclusions such as polyhedral bodies (carboxysomes), ribosomes, and polyphosphate granules were found in Prochlorothrix hollandica. Another type of cell inclusions was identified by its characteristic shape (a cylindre with conical caps) and a regular striation as gas vesicles. It is concluded that the organism is in its morphological structure similar to the cyanobacteria.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-072X
    Keywords: Key words: Cyanobacteria – Outer membrane – Peptidoglycan-associated protein – Pore-forming protein – Porin –Synechococcus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Pore-forming protein (porin) was isolated from N,N-dimethyl-dodecylaminoxid (LDAO)-extracted outer membranes of Synechococcus PCC 6301 and purified by ion exchange chromatography on DEAE-Sephacel column. The apparent molecular mass on SDS-PAGE was determined to be about 52 000. The native porin was reconstituted into black lipid bilayer membranes and showed a single-channel conductance of 5.5 nS in 1 M KCl. The porin was found to be N-terminally blocked. The C-terminal amino acid sequence was identified as Phe-Thr-Phe. Amino acid analysis suggested that the porin protein consists of about 420 amino acid residues, yielding a polarity of 43.6% and a molecular mass of 45 000 in contrast to the mobility on SDS-PAGE.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Experimental brain research 10 (1970), S. 532-554 
    ISSN: 1432-1106
    Keywords: Electrical brain stimulation ; Evoked vocalization ; Saimiri sciureus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Specific vocalization types following electrical stimulation of 5940 electrode positions are studied in 39 squirrel monkeys. Except cerebellum, caudal medulla, and a few cortical areas, the sites of stimulation were distributed throughout the brain. Each vocalization elicited was tested for reproducibility at the site of stimulation and in homologue structures. All vocalizations were analyzed spectrographically and then classified for eight fundamental vocalization types. The cerebral distribution of two call types forms continuous systems extending from midbrain via diencephalon into forebrain; the remaining call types are represented in several separate areas not continuous with each other. In medulla and pons the responsive substrates for vocalization follow the course of the spinothalamic tract; in midbrain they lie within the periaqueductal gray, lateral tegmentum, and lemniscus medialis; in diencephalon they are found in the hypothalamus and midline thalamus; in forebrain, finally they are distributed over amygdala, stria terminalis, substantia innominata, preoptic region, septum, rostral hippocampus, posteromedial orbital cortex, cingulate gyrus, and rostroventral temporal cortex. Hence a close relation between limbic system and vocalization producing substrates emerges. Among the brain structures yielding vocalization the mesencephalic periaqueductal gray is assumed to be the region where the electrical stimulus interferes most directly with specific vocalization mechanisms. Besides the anatomical site of stimulation the set of stimulus parameters is important for the elicitation of vocalizations. Relations between amplitude, frequency, and duration of impulses on the one hand and type, loudness, rhythm, duration, and latency of vocalization on the other hand were tested. The influence of the stimulus set on the reaction parameters depends also on the relative position of the electrode within the effective structure. Proper manipulation of stimulus parameters often results in the disintegration of a complex stimulus response into single components.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 70 (1990), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Triton-insoluble cell walls of the prochlorophyte Prochlorothrix hollandica were isolated by using differential centrifugation of cell homogenates followed by Triton X-100 extraction of the cell envelopes. Polypeptide patterns of solated cell walls were dominated by two major outer membrane proteins with molecular masses of Mr 56 000 and 59 000, respectively. Differential sodium dodecyl sulfate (SDS)-extractions of the cell envelopes yielded SDS-insoluble peptidogly-can-protein complexes which contained both major ofter membrane proteins highly enriched and non-covalently associated with the peptidoglycan layer of Prochlorothrix hollandica.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 92 (1992), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Intracellular localization of triterpenic membrane stabilizers of the hopane series is described for the first time for a cyanobacterium. In Synechocystis PCC 6714, a bacteriohopanetetrol derivative (main compound) and diplopterol were detected in cell wall (CW) and thylakoid membrane (TM). Both hopanoids were enriched 4.5-fold and 9.0-fold in CW and outer membrane (OM) fractions, respectively, compared to TMs.
    Type of Medium: Electronic Resource
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