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KMID : 0380219940270010006
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 1 p.6 ~ p.12
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Purification and Characterization of a 55 kDa Sialoglycoprotein from Rat Liver Lysosomal Membranes
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Abstract
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Abstract:
@EN 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
DEAE-chromatogrphy, and preparative polyacrylamide gel electrophoresis. The purified sialoglycoprotein has a molecular mass of 55kDa(LGP55), as determined by polyacrylamide gel electrophoresis in the presence and absence of SDS, Susceptibility to
neuraminidase 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
olgosaccharide chains. The ten residues of the N-terminal of purified LGP55 are; Ala-Leu-Gln-Val-Thr-Lys-Tyr-Glu-Asp-Gly.
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