| | 1 | Author
| Heino Diringer, MeinradA. Koch | Requires 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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| default:Reihe_C/36/ZNC-1981-36c-0183_n.pdf | | | | Identifier
| ZNC-1981-36c-0183_n | | | | Volume
| 36 | |
| 2 | Author
| B. Rigitte, S. Chobert | Requires 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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| default:Reihe_C/34/ZNC-1979-34c-0699.pdf | | | | Identifier
| ZNC-1979-34c-0699 | | | | Volume
| 34 | |
| 3 | Author
| H. Janzen, E. Matuszak, E. V. Goldammer, AnnenBundesrepublik Deutschland, H. R. Wenzel | Requires 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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| default:Reihe_C/43/ZNC-1988-43c-0285.pdf | | | | Identifier
| ZNC-1988-43c-0285 | | | | Volume
| 43 | |
| 4 | Author
| BlahoslavM. Aršálek, Renata Rojíčková | Requires 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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| default:Reihe_C/51/ZNC-1996-51c-0646.pdf | | | | Identifier
| ZNC-1996-51c-0646 | | | | Volume
| 51 | |
| 5 | Author
| Alfons Radunz | Requires 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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| default:Reihe_C/30/ZNC-1975-30c-0484.pdf | | | | Identifier
| ZNC-1975-30c-0484 | | | | Volume
| 30 | |
| 6 | Author
| Alfons Radunz | Requires 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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| default:Reihe_C/32/ZNC-1977-32c-0597.pdf | | | | Identifier
| ZNC-1977-32c-0597 | | | | Volume
| 32 | |
| 7 | Author
| Alfons Radunz | Requires 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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| default:Reihe_C/34/ZNC-1979-34c-1199.pdf | | | | Identifier
| ZNC-1979-34c-1199 | | | | Volume
| 34 | |
| 8 | Author
| Monier Habib, Tadros, Gerhart Drews, Dierk Evers | Requires 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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| default:Reihe_C/37/ZNC-1982-37c-0210.pdf | | | | Identifier
| ZNC-1982-37c-0210 | | | | Volume
| 37 | |
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