LAMP-1 in cho cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin

• Published in: Biochemical and biophysical research communications Vol. 173; no. 3; pp. 1123 - 1128
• Main Authors: Do, Ki-Young, Smith, David F., Cummings, Richard D.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 31.12.1990; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Antigens, CD; Biological and medical sciences; Carbohydrate Sequence; Cell Line; Chromatography, Affinity; Cricetinae; Cricetulus; Fundamental and applied biological sciences. Psychology; Glycoproteins; Lectins - metabolism; Lysosomal Membrane Proteins; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - metabolism; Molecular Sequence Data; Molecular Weight; Polysaccharides - chemistry; Proteins; PBS; LAMP; PL; L14; Lectin; Vertebrata; Immunoprecipitation reaction; Mammalia; Affinity chromatography; Rodentia; Lysosome; Glycoproteins; Hamster; CHO cell line; Biological receptor

Recent studies indicate that some mammalian S-type lectins bind preferentially to oligosaccharides containing the repeating disaccharide [3Galβ1,4GlcNAcβ1] n or poly-N-acetyllactosamine (PL) sequence. We report here our investigation on the distribution of these sequences in glycoproteins in Chinese...