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1979 (1)
1976 (1)
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    Marvin Stromer, Wilhelm HasselbadhRequires cookie*
 Title    Fusion of Isolated Sarcoplasmic Reticulum Membranes  
 Abstract    Fragmented sarcoplasmic reticulum (FSR) vesicles from rabbit muscle were suspended in 1.5 — 5% glycerol solutions and were pelleted onto aluminum foil disks in a modified centrifuge tube. Examination of these pellets in the electron microscope after drying for 2 — 2.5, 4 — 5.5, and 21 hours revealed a progression of changes. First, distances between individual, round vesicles decreases. Next, somewhat flattened vesicles establish limited areas of contact with adjacent vesicles. Finally, vesicle fusion occurs and extended areas of double bilayers are formed. A water loss-time interaction appears to be needed for the fusion process. A Hg-phenyl azoferritin com­ pound was used as a marker to identify intra-and extra-vesicular space in the fused samples. Quantitative measurements of birefringence during imbibition of pellet slices in a graded series of glycerol solutions indicates a steadily increasing amount of birefringence until 60 — 80% glycerol (»/ = 1.41 —1.43) is readied. The plateau seen in this part of the curve is again followed by steadily increasing birefringence at higher glycerol concentrations. This interruption in the birefringence curve is presumably due to a matching of the refractive indices of the glycerol solution and a lipid component in the membranes. 
  Reference    (Z. Naturforsch. 31c, 703 [1976]; received August 23 1976) 
  Published    1976 
  Keywords    Membrane Fusion, Sarcoplasmic Reticulum, Glycerol, Electron Microscopy, Polarizing Microscopy 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0703.pdf 
 Identifier    ZNC-1976-31c-0703 
 Volume    31