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'Polyacrylamid Gelelectrophoresis' in keywords
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1980 (1)
1Author    Abteilung Biochemie, C.H Boehringer SohnRequires cookie*
 Title    B. Schöbel und W. Pollmann  
 Abstract    In addition to our previous paper [1] further characteristics of the chlorogenic acid hydrolase are described. Polyacrylamid gelelectrophoresis revealed only one band for the purified enzyme. Sodium dodecyl-sulfate polyacrylamid gelelectrophoresis showed a molecular weight of 60000, demonstrating four subunits o f the enzyme (total molecular weight 240000). The enzyme is stable in a pH-range of 3 .0 -8 .5 and up to a temperature o f 55 °C. The temperature coefficient Q10 is 1.5, the activation energy EA is 6.0 kcal/mol. The amino acid analysis and substrate specificity data are given in tables. Essential for the enzyme activity is the C=C double bound neighbouring the ester linkage. The enzyme crystallizes in prisms. Weitere Charakterisierung einer Chlorogensäure-Hydrolase aus Aspergillus niger 
  Reference    Z. Naturforsch. 35c, 699—701 (1980); eingegangen am 12. Mai/20. Juni 1980 
  Published    1980 
  Keywords    Chlorogenic Acid Hydrolase, Aspergillus niger, Polyacrylamid Gelelectrophoresis, Amino Acid Analysis, Substrate Specificity 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0699.pdf 
 Identifier    ZNC-1980-35c-0699 
 Volume    35