Journal article

ISOLATION OF TRANSFERRIN FROM PORCINE GASTRIC-MUCOSA - COMPARISON WITH PORCINE SERUM TRANSFERRIN

GS BALDWIN, T BACIC, R CHANDLER, B GREGO, J PEDERSEN, RJ SIMPSON, BH TOH, J WEINSTOCK

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | PERGAMON-ELSEVIER SCIENCE LTD | Published : 1990

Abstract

1. An iron-binding glycoprotein has been purified to homogeneity from porcine gastric mucosa. 2. The molecular weight (80,000), amino acid composition, carbohydrate content, N-terminal amino acid sequence, tryptic map, stoichiometry of iron binding (2 mol/mol), visible absorption spectrum of the ferric complex and chromatographic behaviour of the gastric protein are all strikingly similar to the corresponding properties of porcine serum transferrin. 3. The quantity of the gastric protein (1.3 mg/g wet weight) present in the gastric mucosa suggests that it is not serum transferrin (plasma concentration 1.8 mg/ml) contaminating the tissue. 4. A role for transferrin in the uptake of dietary iro..

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