Isolation, purification and characterization of porcine serum transferrin and hemopexin.
Two techniques are described for the isolation of porcine serum transferrin and hemopexin, respectively, yielding nearly pure proteins (> 99%) as tested with crossed immunoelectrophoresis. Porcine transferrin has an estimated molecular weight of 79 kDa and porcine hemopexin a molecular weight of 62 kDa. Both purified proteins were subjected to amino acid and carbohydrate analyses. Based on carbohydrate and sialic acid analyses, it is proposed that transferrin contains one bi-antennary glycan chain, whereas hemopexin contains two bi-antennary and one tri-antennary glycan chains.
van Gelder
W
W
Department of Chemical Pathology, Erasmus University Rotterdam, The Netherlands.
Huijskes-Heins
M I
MI
Hukshorn
C J
CJ
de Jeu-Jaspars
C M
CM
van Noort
W L
WL
van Eijk
H G
HG
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002240:Carbohydrate Sequence; D006466:Hemopexin / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013552:Swine; D014168:Transferrin / Q000737:chemistry / Q000302:isolation & purification*
D000596:Amino Acids; D014168:Transferrin; D006466:Hemopexin