Further studies on bovine serum amylase. 3. Affinity chromatography

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Abstract

The major bovine serum isoamylases controlled by the AmI locus have been examined by gel filtration. On Sephadex G-200 the isoamylases can be resolved into two classes. The AmI A and AmI B have apparent molecular weights of 307,000 daltons whilst the AmI C isozyme has an apparent molecular weight of 44,400 daltons. The separation of the isozymes into two classes according to their elution behaviour on Sephadex G-200 has been shown to be an affinity separation. All three AmI isozymes are eluted from a non-dextran media (BioGel A1.5m) with apparent molecular weights of 417,000 daltons. The affinity separation on Sephadex G-200 has been shown to be inhibited by the addition of 1% (w/v) maltose to the elution buffer. In the presence of 1% (w/v) maltose all three AmI isozymes are coeluted from Sephadex G-200 with apparent molecular weights of 321,000 daltons. The maltase and amylase activities of the AmI isozymes were eluted coincidentally under all the conditions studied.
Original languageEnglish
Pages (from-to)71-80
Number of pages10
JournalAnimal blood groups and biochemical genetics
Volume13
Issue number2
Publication statusPublished - 1982

Keywords

  • Amylases
  • Animals
  • Cattle
  • Chromatography, Affinity
  • Chromatography, Gel
  • Isoenzymes

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