Studies of rabbit serum transferrin.
Rabbit serum transferrin is isolated by a procedure designed to preserve its conformation and disulfide linkages. A progress report is presented on the determination of its amino acid sequence, as part of studies on its primary, secondary and tertiary structure. The sequence of 378 residues, of the approximately 680 residues in the molecule, are determined. Observations are made on the site of carbohydrate attachment, iron binding sites and half-cystine residue location. The results are discussed in relation to the X-ray crystallographic studies of human lactoferrin (lactotransferrin) and of rabbit serum transferrin being made in other laboratories.
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John Curtin School of Medical Research, Institute of Advance Studies, Australian National University, Canberra, A.C.T.
McKenzie
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Shaw
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D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002241:Carbohydrates / Q000032:analysis; D007501:Iron / Q000378:metabolism; D008969:Molecular Sequence Data; D011817:Rabbits; D014168:Transferrin / Q000032:analysis*
D002241:Carbohydrates; D014168:Transferrin; D007501:Iron