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Purification of human intrinsic factor using high‐performance ion‐exchange chromatography as the final step
Author(s) -
Gueant Jean-Louis,
Kouvonen Ilkka,
Michalski Jean-Claude,
Masson Catherine,
Gräsbeck Ralph,
Nicolas Jean-Pierre
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80643-8
Subject(s) - ion chromatography , chromatography , chemistry , ion exchange , ion , organic chemistry
Human intrinsic factor was purified 1430‐fold from gastric juice with a yield of 75% using two steps: labile ligand affinity chromatography and high‐performance ion‐exchange chromatography. Intrinsic factor precipitated in the presence of specific autoantibodies and 15% sodium sulfate, had an estimated M r of 59000 in 5% SDS electrophoresis and could bind to the specific ileal receptor in vitro. Its carbohydrate composition could be related to N ‐lactosaminic and O ‐glycosidic chains. High‐performance ion‐exchange chromatography was a mild, rapid and efficient procedure to separate completely intrinsic factor from haptocorrin (another glycoprotein of gastric juice which binds cobalamin) and from other contaminating proteins.