Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Double labeling of transferrin: tritium labeling of sialic acid and /sup 125/I or /sup 59/Fe labeling of the protein moiety

Journal Article · · Anal. Biochem.; (United States)

A method is described in which the glycoprotein transferrin was double labeled. Its sialic acid residues were labeled with /sup 3/H through a consecutive oxidation-reduction technique utilizing tritiated NaBH/sub 4/. Its protein moiety was labeled with either /sup 125/I or /sup 59/Fe. Incubation of this double-labeled molecule at 4/sup 0/C with K562 cells gave overlapping curves, indicating identical patterns of binding for all labels. At 37/sup 0/C, /sup 3/H and /sup 125/I demonstrated identical patterns while /sup 59/Fe was cummulatively retained. This method can be used to follow the fate of other glycoproteins and their possible desialation in vivo.

Research Organization:
Univ. of Mississippi Medical Center, Jackson
OSTI ID:
5496719
Journal Information:
Anal. Biochem.; (United States), Journal Name: Anal. Biochem.; (United States) Vol. 153:2; ISSN ANBCA
Country of Publication:
United States
Language:
English