ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase.

Samankaltaisia teoksia

• Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit.
  Tekijä: Veijola, J, et al.
  Julkaistu: (1996)
• Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene.
  Tekijä: Pihlajaniemi, T, et al.
  Julkaistu: (1987)
• Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit.
  Tekijä: Helaakoski, T, et al.
  Julkaistu: (1995)
• Co-expression of the alpha subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes. Soluble alpha-subunit-BiP complexes have no prolyl 4-hydroxylase activity.
  Tekijä: Veijola, J, et al.
  Julkaistu: (1996)
• Molecular cloning of a multifunctional chicken protein acting as the prolyl 4-hydroxylase beta-subunit, protein disulphide-isomerase and a cellular thyroid-hormone-binding protein. Comparison of cDNA-deduced amino acid sequences with those in other species.
  Tekijä: Parkkonen, T, et al.
  Julkaistu: (1988)