5
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Identification of sialyl and galactosyl transferase activities in calf vitreous hyalocytes.

      Current Eye Research

      Animals, Cattle, Chromatography, Gel, methods, Clostridium perfringens, enzymology, Culture Media, Galactosyltransferases, isolation & purification, In Vitro Techniques, Macrophages, Mucins, diagnostic use, Neuraminidase, Sialyltransferases, Solubility, Submandibular Gland, secretion, Transferases, Tritium, Vitreous Body, cytology, beta-Galactosidase

      Read this article at

      ScienceOpenPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Sialyl and galactosyl transferase activities are demonstrated in calf vitreous hyalocytes. For study of sialyl transferase activity, a partially purified vitreous preparation (collagen and hyaluronic acid removed), and bovine submaxillary mucin were treated with an insolubilized neuraminidase before use acceptor of radioactivity from CMP-[3H]-N-acetylneuraminic acid (CMP-[3H]-NAN). For study of galactosyl transferase activity the vitreous preparation was treated first with insolubilized neuraminidase and then with an insolubilized beta-galactosidase before use as acceptor of radioactivity from UDP-[3H]-galactose (UDP-[3H]-gal). Galactosyl transferase requires a divalent metal ion for optimal activity, and the reactions catalyzed by each enzyme are dependent upon pH, time of incubation and concentration of enzyme and/or acceptor.

          Related collections

          Author and article information

          Journal
          6091999

          Comments

          Comment on this article