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Different half-lives of the carbohydrate and protein moieties of a 110,000-dalton glycoprotein isolated from plasma membranes of rat liver.

Authors
  • Kreisel, W
  • Volk, B A
  • Büchsel, R
  • Reutter, W
Type
Published Article
Journal
Proceedings of the National Academy of Sciences of the United States of America
Publication Date
Apr 01, 1980
Volume
77
Issue
4
Pages
1828–1831
Identifiers
PMID: 6929523
Source
Medline
License
Unknown

Abstract

By using a four-step procedure (i, solubilization with Triton X-100; ii, affinity chromatography on concanavalin A-Sepharose; iii, affinity chromatography on wheat germ lectin-Sepharose; iv, preparative sodium dodecyl sulfate gel electrophoresis) a glycoprotein was isolated from rat liver plasma membrane. The molecular weight is 110,000 and the isoelectric point is 5.8. It contains L-fucose, N-acetylneuraminic acid, D-galactose, D-mannose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, and considerable quantities of aspartate, threonine, serine, and leucine. In pulse-chase experiments the half-lives of methionine and arginine, representing the half-life of the protein, were determined as 70 hr and 78 hr, respectively. The half-lives of the terminal carbohydrates L-fucose and N-acetylneuraminic acid were 12.5 and 33 hr, respectively. The galactose half-life was 20 hr. From this it is concluded that terminal sugars turn over several times in the life-span of this protein molecule. This process may be operative during membrane recycling mechanisms.

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