Isolation of transferrin from porcine gastric mucosa: comparison with porcine serum transferrin.
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 iron by the gastrointestinal tract is proposed.
Baldwin
G S
GS
Ludwig Institute for Cancer Research, P.O. Royal Melbourne Hospital, Victoria, Australia.
Bacic
T
T
Chandler
R
R
Grego
B
B
Pedersen
J
J
Simpson
R J
RJ
Toh
B H
BH
Weinstock
J
J
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000645:Ammonium Sulfate; D000818:Animals; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D005753:Gastric Mucosa / Q000032:analysis*; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009005:Monosaccharides / Q000032:analysis; D010449:Peptide Mapping; D011485:Protein Binding; D011863:Radioimmunoassay; D013053:Spectrophotometry; D013552:Swine; D014168:Transferrin / Q000302:isolation & purification*; D014357:Trypsin
D000596:Amino Acids; D009005:Monosaccharides; D014168:Transferrin; D014357:Trypsin; D000645:Ammonium Sulfate