Evidence for the glycosylation of porcine serum transferrin at a single site located within the C-terminal lobe.
In this study we report the number and location of the glycans on PST. Urea PAGE and SDS-PAGE have been used to follow the enzymatic removal of sialic acids and of glycans from PST and the masses of native and deglycosylated PST have been determined by electrospray mass spectrometry. The results are consistent with the presence of a single biantennary glycan chain. As amino acid sequence analysis demonstrated the absence of a glycosylated asparagine at position 25, the glycosylation site is restricted to Asp-497.
Sharma
N D
ND
Division of Biochemistry and Molecular Biology, UMDS, Guy's Hospital, London, UK.
Evans
R W
RW
Patel
K J
KJ
Gorinsky
B
B
Mallet
A I
AI
Aitken
A
A
D000595:Amino Acid Sequence; D000818:Animals; D006026:Glycoside Hydrolases; D006031:Glycosylation; D008969:Molecular Sequence Data; D009439:Neuraminidase; D011134:Polysaccharides / Q000032:analysis; D012794:Sialic Acids / Q000032:analysis; D013552:Swine; D014168:Transferrin / Q000737:chemistry* / Q000302:isolation & purification
D011134:Polysaccharides; D012794:Sialic Acids; D014168:Transferrin; D006026:Glycoside Hydrolases; D009439:Neuraminidase