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1987 (1)
1983 (1)
1Author    JaquesR. Abier, M. Ookam, Besw Aran, V. Ijayalakshm, W. Olfhart, R. ÜdigerRequires cookie*
 Title    Affinity of Phycocyanin Chromopeptides to Histidyl-Sepharose Gels: A Model for Histidine-Tetrapyrrol-Interactions in Biliproteins  
 Abstract    C-Phycocyanin from the cyanobacterium Spirulina m axim a was digested with pepsin to yield chromopeptides and colorless peptides. This mixture was applied to columns o f histidyl-Sepha-roseunder a variety of conditions (pH-value, ionic strength of buffer). We found a good separa­ tion of several chrom opeptides from each other and from colorless peptides due to differential interaction of phycocyanobilin chrom ophore with the histidyl residue o f the gel. The separation is suppressed by the use of imidazole buffer. Control experiments were perform ed with purified chromopeptides and with octyl-Sepharose and DEAE-Sepharose. The nature of interaction which probably involves charge transfer interaction besides hydrophobic and ionic forces is discussed with regard to the significance for phytochrome. 
  Reference    Z. Naturforsch. 38c, 230—236 (1983); received N ovember 22 1982 
  Published    1983 
  Keywords    Phycocyanobilin-Peptides, Histidyl-Sepharose, Octyl-Sepharose, DEAE-Sepharose, Gel Filtration 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0230.pdf 
 Identifier    ZNC-1983-38c-0230 
 Volume    38 
2Author    A. Lberto Mazzini, R. Oberto FavillaRequires cookie*
 Title    The Effect of Guanidinium Chloride on the Self-Association of Bovine Liver Glutamate Dehydrogenase: A Gel Filtration Study  
 Abstract    The associative behaviour of bovine liver glutamate dehydrogenase has been studied by gel chrom atography at neutral pH in 1 m guanidinium chloride and 1 m sodium chloride. In guanidinium chloride both the elution volume and the elution profile of the enzyme are independ­ ent of protein concentration, whereas in sodium chloride they are strongly dependent on it. In NaCl the enzyme behaves as expected according to the well established random association m odel, w hereas in guanidinium chloride it appears to have completely lost the self-associative property. F urtherm ore, since the elution volume of the enzyme in guanidinium chloride corre­ sponds to that of an hexamer, trim er formation reported to occur in these conditions is not confirmed !?'7 this technioue 
  Reference    Z. Naturforsch. 42c, 217 (1987); received O ctober 17 1986 
  Published    1987 
  Keywords    G lutam ate D ehydrogenase, Self-Association, Guanidine Chloride, Inactivation, Gel Filtration 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0217.pdf 
 Identifier    ZNC-1987-42c-0217 
 Volume    42