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Purification and Characterization of a 55kDa Sialoglycoprotein from Rat Liver Lysosomal Membranes
Joon Kyum Kim,Masaru Himeno,Keitaro Kato Mie Young Kim 생화학분자생물학회 1994 BMB Reports Vol.27 No.1
A sialoglycoprotein was purified to apparent homogeneity from rat liver lysosomal membranes with a 0.1% recovery by WGA-Sepharose 6B, Con A-Sepharose, and Hydroxylapatite chromatography, Superdex TM200 FPLC gel filtration, TSK-5PW FPLC DEAF-chromatogrphy, and preparative polyacrylamide gel electrophoresis. The purified sialoglycoprotein has a molecular mass of 55 kDa (LGP55), as determined by polyacrylamide gel electrophoresis in the presence and absence of SDS. Susceptibility to neurnminidase and endoglycosidase H, and the immunoreactivity of the protein in tritosome membranes was examined in order to study the topology of the lysosomal membrane. The results suggest that LGP55 is an intact lysosomal membrane protein with oligosaccharide chains. The ten residues of the N-terminal of purified LGP55 are ; Ala-Leu-Gln-Val-Thr-Lys-Tyr-Glu-Asp-Gly.