Structural similarity between the macrophage lectin specific for galactose/N-acetylgalactosamine and the hepatic asialoglycoprotein binding protein.
The rat peritoneal macrophage lectin specific for galactose/N-acetylgalactosamine was shown to be a homologue of the hepatic asialoglycoprotein binding protein (rat hepatic lectin, RHL). The macrophage lectin was immunochemically crossreactive with the major form of RHL (RHL-1) but not with the minor forms (RHL-2 and -3). The overall homology between the macrophage lectin and RHL-1 was confirmed by peptide maps of their lysyl endopeptidase digests on reverse-phase HPLC. Despite these similarities, however, the macrophage lectin was distinct from HRL-1 as revealed by the differences in the NH2-terminal 20 amino acid sequences of these two lectins.
Ii
M
M
Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Kawasaki
T
T
Yamashina
I
I
D000116:Acetylgalactosamine / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000032:analysis*; D002851:Chromatography, High Pressure Liquid; D005688:Galactosamine / Q000031:analogs & derivatives*; D005690:Galactose / Q000378:metabolism*; D007150:Immunohistochemistry; D037102:Lectins; D008264:Macrophages / Q000032:analysis*; D010449:Peptide Mapping; D051381:Rats; D011956:Receptors, Cell Surface
D002352:Carrier Proteins; C023339:Clec10a protein, rat; D037102:Lectins; D011956:Receptors, Cell Surface; D005688:Galactosamine; D000116:Acetylgalactosamine; D005690:Galactose