The high occurrence in large intestine epithelial cells from pig of a beta-N-acetylgalactosaminyltransferase with a substrate specificity very similar to that of the Sda beta 1,4-N-acetylgalactosaminyltransferase from other tissues is reported. The enzyme strictly recognized the NeuAc alpha 2,3Gal beta terminal sequence of N- and O-linked oligosaccharides bound to glycoproteins. The transferase activity required Mn2+ and an optimum pH of 7.4. In contrast to the kidney Sda-enzyme from humans and other mammals, the microsomal fraction of pig colonic cells expressed a very high activity even in the absence of Triton X-100. A rapid procedure is presented for the large scale preparation of GalNAc beta 1,4(NeuAc alpha 2,3)Gal beta 1,4Glc from NeuAc alpha 2,3Gal beta 1,4Glc. The biosynthesized tetrasaccharide was completely resistant to the action of neuraminidase from Vibrio cholerae, whereas about 60% of N-acetylneuramic acid was cleaved by neuraminidase from Newcastle disease virus. HPLC separation of different compounds is reported

Nadia Malagolini, Fabio Dall'olio, Stefania Guerrini, Franca Serafini-Cessi (1994). Identification and characterization of the Sda beta1,4,N-acetylgalactosaminyltransferase from pig large intestine. GLYCOCONJUGATE JOURNAL, 11(2), 89-95 [10.1007/bf00731148].

Identification and characterization of the Sda beta1,4,N-acetylgalactosaminyltransferase from pig large intestine

Nadia Malagolini;Fabio Dall'olio;
1994

Abstract

The high occurrence in large intestine epithelial cells from pig of a beta-N-acetylgalactosaminyltransferase with a substrate specificity very similar to that of the Sda beta 1,4-N-acetylgalactosaminyltransferase from other tissues is reported. The enzyme strictly recognized the NeuAc alpha 2,3Gal beta terminal sequence of N- and O-linked oligosaccharides bound to glycoproteins. The transferase activity required Mn2+ and an optimum pH of 7.4. In contrast to the kidney Sda-enzyme from humans and other mammals, the microsomal fraction of pig colonic cells expressed a very high activity even in the absence of Triton X-100. A rapid procedure is presented for the large scale preparation of GalNAc beta 1,4(NeuAc alpha 2,3)Gal beta 1,4Glc from NeuAc alpha 2,3Gal beta 1,4Glc. The biosynthesized tetrasaccharide was completely resistant to the action of neuraminidase from Vibrio cholerae, whereas about 60% of N-acetylneuramic acid was cleaved by neuraminidase from Newcastle disease virus. HPLC separation of different compounds is reported
1994
Nadia Malagolini, Fabio Dall'olio, Stefania Guerrini, Franca Serafini-Cessi (1994). Identification and characterization of the Sda beta1,4,N-acetylgalactosaminyltransferase from pig large intestine. GLYCOCONJUGATE JOURNAL, 11(2), 89-95 [10.1007/bf00731148].
Nadia Malagolini; Fabio Dall'olio; Stefania Guerrini; Franca Serafini-Cessi
File in questo prodotto:
Eventuali allegati, non sono esposti

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/903480
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? 4
  • Scopus ND
  • ???jsp.display-item.citation.isi??? ND
social impact