Separation and characterization of the C-terminal half molecule of bovine lactoferrin.
The C-terminal half molecule (C lobe) of bovine lactoferrin was isolated by mild tryptic hydrolysis of lactoferrin followed by gel filtration and ion-exchange chromatography. The identity of the fragment was established by determining its N-terminal and C-terminal amino acid sequences and comparing them with the amino acid sequence of intact lactoferrin. The isoelectric point of the C lobe ranged between pH 6.2 and 6.5 as measured by isoelectric focusing on polyacrylamide gels. The circular dichroic spectrum in the range of 250 to 350 nm of the C lobe differed slightly from that of intact lactoferrin. The pattern of lectin reactivity was similar for both the C lobe and intact lactoferrin. The C lobe showed partial antigenic identity with intact lactoferrin as demonstrated by the double immunodiffusion method, and pH dependence of iron binding of C lobe is the same as that of intact lactoferrin molecule.
Shimazaki
K
K
Protein Chemistry Section, Obihiro University of Agriculture and Veterinary Medicine, Japan.
Tanaka
T
T
Kon
H
H
Oota
K
K
Kawaguchi
A
A
Maki
Y
Y
Sato
T
T
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007526:Isoelectric Point; D007781:Lactoferrin / Q000737:chemistry / Q000302:isolation & purification*; D037102:Lectins / Q000378:metabolism; D008892:Milk / Q000737:chemistry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification*; D014357:Trypsin / Q000378:metabolism
D037102:Lectins; D010446:Peptide Fragments; D007781:Lactoferrin; D014357:Trypsin