Cellular localization of the galactose-binding lectin from human serum.
An SL2 lectin was isolated from human serum and characterized previously; cellular localization of the lectin was studied using polyclonal rabbit antibodies. According to cytofluorimetry, anti-SL2 antibodies bound only to lymphocytes and monocytes but not to other blood cells. Antibodies bound to Jurkat T cell lymphoma but did not interact with IM-9 cells of B cell origin. Moreover, the Jurkat cells bound oligosaccharides having the highest affinity to SL2 (GalNAcalpha_and Fucalpha1-2Gal), and this interaction was inhibited by anti-SL2 antibodies. Lysis of the Jurkat cells with subsequent electrophoresis and Western blotting indicates that anti-SL2 antibodies recognized a 14-kD protein.
Rapoport
E M
EM
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117871, Russia. rapoport@mail.ibch.ru
Nekrasov
M V
MV
Khaidukov
S V
SV
Svirshchevskaya
E V
EV
Zhigis
L S
LS
Kozlov
L V
LV
Batalova
T N
TN
Zubov
V P
VP
Bovin
N V
NV
D000818:Animals; D006801:Humans; D019169:Jurkat Cells; D037102:Lectins / Q000097:blood* / Q000276:immunology; D011817:Rabbits; D013050:Spectrometry, Fluorescence
D037102:Lectins