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1Author    Heino Diringer, MeinradA. KochRequires cookie*
 Title    The Specific Labeling in H ypertonic M edium o f a Spleen Protein  
 Abstract    The biosynthesis of a 12000 dalton protein species released into the medium by mouse spleen was resistant to the inhibitory effect of hypertonic medium on protein syn­ thesis. This protein fraction comprised 10% or more o f the total radioactive protein in the medium but could hardly be detected in the spleens. It was labeled very often to a higher extent in diseased animals. It is not related antigen-ically to either /?-microglobin, mouse-interferon, or to mouse immuno-globulins. A preferential uptake into cells of certain organs, which, when themselves incubated in organ cultures did not synthesize and release the protein, was observed. 
  Reference    Z. Naturforsch. 36c, 183—188 (1981); received September 11/November 13 1980 
  Published    1981 
  Keywords    Spleen, Mouse, Protein 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0183_n.pdf 
 Identifier    ZNC-1981-36c-0183_n 
 Volume    36 
2Author    L. Ya, E. W. Baranov, SchlagRequires cookie*
 Title    New Mechanism for Facile Charge Transport in Polypeptides  
 Abstract    An electronic hole migration accross a polypeptide chain is discussed with special reference to new ab initio computational results and to the experimental observations of Weinkauf et al. on the charge photoinjection into the polypeptide backbone. New mechanistic details for this efficient charge transport process are proposed. The process is viewed as a vibronically induced hole hopping between local aminoacid sites driven by large amplitude torsional motions of the floppy backbone. 
  Reference    Z. Naturforsch. 54a, 387—396 (1999); received May 7 1999 
  Published    1999 
  Keywords    Protein, Polypeptide, Charge Transfer, Hopping 
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 TEI-XML for    default:Reihe_A/54/ZNA-1999-54a-0387.pdf 
 Identifier    ZNA-1999-54a-0387 
 Volume    54 
3Author    Friederike Koenig, Wilhelm Menke, Hans Craubner, GeorgH. Schmid, Alfons RadunzRequires cookie*
 Title    Photochemically Active Chlorophyll-Containing Proteins from Chloroplasts and their Localization in the Thylakoid Membrane  
 Abstract    After solubilization of stroma-freed chloroplasts with deoxycholate, the lipids and the detergent used are separated from the proteins by gel filtration. In this way not denatured pigment-con-taining protein preparations were obtained. The particles in fraction 1 exhibited a molecular weight of 600 000 and contained an average of 25 chlorophyll molecules. The circular dichroism spectrum showed exciton splitting of the red band. The particles in fraction 2 contained 1 chloro-phyll molecule and exhibited a molecular weight of 110 000. The particles in fraction 3 also contained only 1 chlorophyll molecule and had a molecular weight of between 80 000 and 100 000. Pure preparations of fraction 1 only carried out the methylviologen M e h 1 e r reaction with the dichlorophenol indophenol/ascorbate couple as electron donor. Fraction 3 only reduced ferri-cyanide with diphenylcarbazide as an electron donor in the light. Fraction 2 exhibited both the photosystem I reaction and the photosystem II reaction. An antiserum to extracted fraction 1 does not inhibit electron transport in the intact lamellar system. The photoreduction of methylviologen is only inhibited after disruption of the thylakoids. The antiserum to fraction 2 inhibits the photo-reduction of methylviologen in the intact lamellar system. Consequently, one inhibition site for this photosystem I reaction must be located on the inner and another on the outer surface of the thylakoid membrane. In addition, antibodies to fraction 1 are specifically adsorbed onto the lamellar system without any effect on electron transport and without a concomitant agglutination. Antibodies to fraction 3 partially inhibit the photoreduction of ferricyanide with diphenylcarbazide as an electron donor in the intact lamellar system. Hence, the inhibition site of this system II reaction is located on the outer surface of the thylakoids. We have reason to believe that the inhibition sites not reacting are located in the partitions, which are not accessible to antibodies. 
  Reference    (Z. Naturforsch. 27b, 1225 [1972]; received July 5 1972) 
  Published    1972 
  Keywords    Chloroplasts, membranes, proteins, photosynthesis, antibodies 
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 TEI-XML for    default:Reihe_B/27/ZNB-1972-27b-1225.pdf 
 Identifier    ZNB-1972-27b-1225 
 Volume    27 
4Author    G. SegewitzRequires cookie*
 Title    Liganden-und Isotopenaustausch im System: Serumproteine — Zink — Polyaminopolycarbonsäuren Ligand and Isotope Exchange in the System: Serum Proteins — Zinc — Polyaminopolycarbonic Acids  
 Abstract    In vitro-studies show that the Ca-chelates of EDTA and DTPA are equally effective in removing Zn from the proteins and that the Zn-protein pool is composed of several fractions with different stabilities. Only a small fraction of the protein-bound Zn can be labelled by 65 Zn in vitro and, as to the mobilization of 65 Zn, Ca-DTPA was found to be 20 times more effective than equimolar Ca-EDTA. The isotope exchange between Zn-DTPA and protein-bound 65 Zn is an extremely fast reaction whereas in the case of Zn-EDTA a sluggish exchange takes place. The analysis of the results led to conclusion that the ligand and isotope exchange reactions in the case of EDTA proceed via the free Zn 2+ -ion; with the high-dentate DTPA, however, the formation of ternary and mixed complexes plays an important role. The implications of the findings as related to the toxi-city of the Ca-chelates are discussed. 
  Reference    (Z. Naturforsch. 27b, 1370—1375 [1972]; eingegangen am 14. Juli 1972) 
  Published    1972 
  Keywords    Zinc, Radiozinc, Proteins, Ethylenediaminetetraacetate, Diethylenetriaminepentaacetate 
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 TEI-XML for    default:Reihe_B/27/ZNB-1972-27b-1370.pdf 
 Identifier    ZNB-1972-27b-1370 
 Volume    27 
5Author    B. Rigitte, S. ChobertRequires cookie*
 Title    A Near-Infrared Spectroscopic Investigation of Water in Solutions with Proline, Glycinebetaine, Glycerol and Albumin  
 Abstract    The (v2 + v3) com bination band o f water has been investigated in aqueous solutions o f proline, glycinebetaine and glycerol and in a three component solution with each o f these substances and albumin. It is shown that the hydrogen bonding strength between the water protons and proline or betaine is higher than between water and glycerol. Betaine exhibits a higher affinity versus the oxygen o f water than does proline. The water binding capacity o f pure proline solutions is unchanged in a three-com ponent solu­ tion with albumin. Proline neither enhances nor reduces the solubility o f this highly soluble pro­ tein. In contrast, in a three-com ponent solution with betaine, the solubility o f both betaine and al­ bum in is reduced. It is assumed that these solute particles com pete for the sam e binding position on the water m olecule. Concentrated glycerol solutions with very low water concentrations dissolve a considerable am ount o f albumin, which points to the fact that the protein must be partly dis­ solved in glycerol itself. 
  Reference    Z. Naturforsch. 34c, 699—703 (1979); received February 2/M ay 29 1979 
  Published    1979 
  Keywords    Water, Protein, Proline, Betaine, Glycerol 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0699.pdf 
 Identifier    ZNC-1979-34c-0699 
 Volume    34 
6Author    H. Janzen, E. Matuszak, E. V. Goldammer, AnnenBundesrepublik Deutschland, H. R. WenzelRequires cookie*
 Title    Thermodynamic and Magnetic Resonance Studies on the Hydration of Polymers: II. Protein-Water Interactions in Powdered Ribonuclease  
 Abstract    ESR studies on spin-labeled amorphous RNase A as a function of varying concentrations of sorbed H 2 0 and D 2 0 will be presented. A relaxation analysis of saturation transfer (ST-)ESR spectra of l4 N('H) nitroxide spin-label molecules essentially fixed at amino acid residue His-105 will be given. A characteristic correlation has been observed between the microdynamic behavior — express-ed by the rotational correlation times of the paramagnetic label — and the macroscopic thermo-dynamic entropy for the sorption process of H 2 0 and D 2 0 at RNase. This correlation is particu-larly pronounced at low water concentrations, viz., n H20 /n protein < 100. A significant difference in this concentration range exists between the two systems "RNase-H 2 0" and "RNase-D 2 0", which is manifested not only by the thermodynamic data but also by the microdynamic behavior ex-tracted from the corresponding non-linear ESR absorption line shapes. 
  Reference    Z. Naturforsch. 43c, 285—293 (1988); received December 18 1987 
  Published    1988 
  Keywords    Protein, Structure, Hydration, NMR, Thermodynamic 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0285.pdf 
 Identifier    ZNC-1988-43c-0285 
 Volume    43 
7Author    BlahoslavM. Aršálek, Renata RojíčkováRequires cookie*
 Title    Stress Factors Enhancing Production of Algal Exudates: a Potential Self-Protective Mechanism?  
 Abstract    Algae are known to produce extracellular organic substances under optimum conditions and increase their production under stress. The changes in amount and composition of extra­ cellular carbohydrates and proteins of three green algae Scenedesmus quadricauda, Chlorella kessleri and Raphidocelis subcapitata (known as Selenastrum capricornutum) were studied after a 5-days' cultivation under the influence of different types o f stress factors (osm otic, organic, and heavy metal stressors). NaCl enhanced the quantity of carbohydrates more than proteins. A higher increase o f proteins than carbohydrates was observed after addition of 3,5-dichlorophenol, glyphosate and cadmium chloride to algal cultures. The production of dissolved organic matter differs from species to species, with the age of a culture and the type of stressor. 
  Reference    Z. Naturforsch. 51c, 646 (1996); received May 28/June 25. 1996 
  Published    1996 
  Keywords    Algae, Extracellular Products, Proteins, Carbohydrates 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0646.pdf 
 Identifier    ZNC-1996-51c-0646 
 Volume    51 
8Author    Alfons RadunzRequires cookie*
 Title    Binding of Antibodies onto the Thylakoid Membrane I. Maximal Antibody Binding and Adsorption of Antibodies to Lipids  
 Abstract    The binding of antibodies onto the lamellar system of A ntirrhinum m ajus was determined in dependence on the serum addition. The unspecific adsorption of serum proteins was taken into account or eliminated. The binding of antibodies as a function of the amount of serum added is seen from a saturation curve. From an antiserum obtained by hyperimmunization with stroma-freed chloroplasts, the chloroplasts bind maximally 1 gram antibodies per gram stroma-freed chloro­ plasts. From an antiserum to the proteins of the thylakoid membrane prepared in the same way an equal amount of antibodies is adsorbed. It is assumed that with this amount the surface of the lamellar system accessible to antibodies is completely covered by antibodies. For an antiserum to monogalactosyl diglyceride a maximal antibody binding of 0.16 g, for sulphoquinovosyl diglyceride 0.12 g and for phosphatidyl glycerol 0.13 g of antibodies per gram stroma-freed chloroplasts are obtained. The significance of these results with respect to the molecular surface structure of the thylakoid membrane is discussed. 
  Reference    (Z. Naturforsch. 30c, 484—488 [1975]; received April 11975) 
  Published    1975 
  Keywords    Chloroplasts, Lipids, Proteins, Antibodies, Membrane Structure 
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 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0484.pdf 
 Identifier    ZNC-1975-30c-0484 
 Volume    30 
9Author    Alfons RadunzRequires cookie*
 Title    Binding of Antibodies onto the Thylakoid Membrane II. Distribution of Lipids and Proteins at the Outer Surface of the Thylakoid Membrane  
 Abstract    The number of antibody molecules which stroma-freed chloroplasts can bind out of the mono-specific antisera to monogalactosyl diglyceride, tri-and digalactosyl diglyceride, sulfoquinovosyl diglyceride, phosphatidyl glycerol, sitosterol, plastoquinone, lutein and neoxanthin was determined. This number was compared to the number of antibody molecules which stroma-freed chloroplasts can maximally bind. The result is that the antibodies to the individual lipids cover at most 17 per cent of the accessible thylakoid membrane surface. From a serum which contains both antibodies to the proteins and lipids of the thylakoid mem­ brane, not more antibody molecules are bound than from a serum to the proteins. This means that antibodies to proteins are able to cover up the entire accessible surface of the thylakoids whereas a mixture of antibodies to the lipids, listed above, cover only one forth of the surface. Consequently, antibodies which are bound to proteins can cover up the lipid areas entirely and in turn antibodies which are bound to lipids cover up parts of the protein areas. From this it follows that the portion of the surface, which is made up by lipids must be considerably smaller than 24 per cent. Furthermore, it follows from these experiments that the lipid areas are small and that lipids probably only fill up the gaps between the protein molecules. 
  Reference    (Z. Naturforsch. 32c, 597 [1977]; received May 6 1977) 
  Published    1977 
  Keywords    Chloroplasts, Lipids, Proteins, Antibodies, Membrane Structure 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0597.pdf 
 Identifier    ZNC-1977-32c-0597 
 Volume    32 
10Author    Alfons RadunzRequires cookie*
 Title    Binding of Antibodies onto the Thylakoid Membrane. V. Distribution of Proteins and Lipids in the Thylakoid Membrane  
 Abstract    Binding of antibodies to proteins and lipids onto fragments of the thylakoid membrane was stu­ died and compared with the binding o f antibodies by stroma-freed chloroplasts. The mem brane fragments were prepared from strom a-free chloroplasts by ultrasonication and fractional cen­ trifugation. The fragments have an average diam eter of 200 A. T heir thickness corresponds to that of the thylakoid membrane. The m em brane fragments adsorb out o f an antiserum to lipids appro­ ximately the same am ount o f antibodies as out of an antiserum to proteins. In comparison to this, stroma-free chloroplasts bind 4 times more antibodies to proteins than to lipids. From this it fol­ lows that the major part o f the lipids is located in the m em brane surface which is directed towards the inside or is located inside the mem brane. As the chemical analysis has shown these results are not caused by an altered chemical composition of the m em brane fragments. Despite the fact that m em brane proteins bind considerably less protein antibodies than stroma-free chloroplasts, the antibody binding in m em brane fragment might be considerably increased for certain proteins such as a polypeptide with an apparent molecular weight 24000 and cytochro­ me f. Antibodies to the m ajor components o f the lipid mixture, such as to monogalactosyl diglyce-ride, trigalactosyl diglyceride, sulfoquinovosyl diglyceride and phosphatidyl glycerol are 3 to 4 times more bound by m em brane fragments than by stroma-free chloroplasts. From these results it is concluded that the thylakoid m em brane surface directed towards the inside is preponderently composed of lipids whereas the surface directed towards the outside consists only by 10 to 15% of lipids. 
  Reference    Z. Naturforsch. 34c, 1199—1204 (1979); received July 6 1979 
  Published    1979 
  Keywords    Chloroplasts, Thylakoid M em brane Surface, Proteins, Lipids, Antibodies 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-1199.pdf 
 Identifier    ZNC-1979-34c-1199 
 Volume    34 
11Author    Monier Habib, Tadros, Gerhart Drews, Dierk EversRequires cookie*
 Title    Peptidoglycan and Protein, the Major Cell Wall Constituents of the Obligate Halophilic Bacterium Rhodospirillum salexigens  
 Abstract    The obligate halophilic member o f Rhodospirillaceae, Rhodospirillum salexigens, does not con­ tain lipopolysaccharide in its thin and delicate gram-negative type cell wall. Major constituents are protein (approximately 70% of dry weight) and peptidoglycan (murein). 
  Reference    Z. Naturforsch. 37c, 210 (1982); received November 20 1981 
  Published    1982 
  Keywords    Murein, Peptidoglycan, Cell Wall, Halophilic, Phototrophic Bacterium, Protein 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0210.pdf 
 Identifier    ZNC-1982-37c-0210 
 Volume    37 
12Author    G. TripathiRequires cookie*
 Title    Thyroid Hormone-Induced Changes in Cytoplasmic and Mitochondrial Proteins of a Teleost  
 Abstract    The effect of triiodothyronine (T 3) on the cytoplasmic and mitochondrial protein contents were studied in the liver and skeletal muscle of a freshwater teleost. The fish exposed to thiouracil for 28 days showed 1 .5 -2 times reduction in the total protein contents of cyto­ plasmic and mitochondrial fractions. A single injection of T 3 to thiouracil exposed fish caused 
  Reference    Z. Naturforsch. 53c, 120 (1998); received June 2/Novem ber 18 1997 
  Published    1998 
  Keywords    Triiodothyronine, Protein, Liver, Skeletal Muscle, Fish 
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 TEI-XML for    default:Reihe_C/53/ZNC-1998-53c-0120.pdf 
 Identifier    ZNC-1998-53c-0120 
 Volume    53 
13Author    Requires cookie*
 Title    Okan Gurel  
 Abstract    It is proposed that the biological communication is a language process with the basic word structure formed as a hexagonal neighborhood on the a-helix region of protein molecules. 
  Reference    (Z. Naturforsch. 30c, 843 [1975]; received) 
  Published    1975 
  Keywords    ) a-Helix, Amino Acids, Proteins, Hexagonal Neighborhood, Biological Communication 
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 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0843_n.pdf 
 Identifier    ZNC-1975-30c-0843_n 
 Volume    30