Isolation and characterization of a sulfated glycoprotein from a transplantable colorectal adenocarcinoma of rats.
A transplantable colorectal adenocarcinoma from rats of the ACI/N strain was extracted with 5 mM EDTA (pH 7.0), and fractionated by gel filtration on Sepharose 4B, followed by preparative poly(vinyl chloride) zone electrophoresis. An acidic glycoprotein (SGP) thus obtained was shown to be Homogeneous by electrophoresis on cellulose acetate membrane and on sodium dodecyl sulfate agarose gel. SGP contained 61.9% carbohydrate, 28.9% total amino acids and 1.4% sulfate. The major monosaccharides in SGP were galactose, glucosamine and galactosamine. Small quantities of sialic acid, L-fucose and mannose were also present. Threonine, serine, proline, glutamic acid and aspartic acid were the major amino acids of the protein moiety.
D000230:Adenocarcinoma / Q000032:analysis*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D051152:Clusterin; D003110:Colonic Neoplasms / Q000032:analysis*; D006023:Glycoproteins / Q000302:isolation & purification; D018832:Molecular Chaperones; D009374:Neoplasms, Experimental / Q000032:analysis; D051381:Rats; D012004:Rectal Neoplasms / Q000032:analysis*; D013055:Spectrophotometry, Infrared
D000596:Amino Acids; D002241:Carbohydrates; D051152:Clusterin; D006023:Glycoproteins; D018832:Molecular Chaperones