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'Protein' in keywords Facet   Publication Year 1979  [X]
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1979[X]
1Author    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 
2Author    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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 DEBUG INFO      
 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-1199.pdf 
 Identifier    ZNC-1979-34c-1199 
 Volume    34