A minor sialoglycoprotein of the human erythrocyte membrane
| Autor: | Thomas J. Mueller, Martin Morrison, J.William Owens |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Gel electrophoresis
Erythrocytes Chromatography biology Chemistry Sialoglycoproteins Erythrocyte Membrane Lactoperoxidase Biophysics Periodate Biochemistry Peptide Fragments Molecular Weight chemistry.chemical_compound Sulfite Thermolysin Sialoglycoprotein biology.protein Humans Glycophorin Trypsin Cyanogen bromide Cyanogen Bromide Molecular Biology |
| Zdroj: | Archives of Biochemistry and Biophysics. 204:247-254 |
| ISSN: | 0003-9861 |
| Popis: | The sialoglycoprotein periodate fuchsin sulfite 2 has about 8% of the sialic acid contained in the sialoglycoproteins of the human erythrocyte membrane. This polypeptide appears to have an apparent monomeric molecular weight of 35,000, somewhat smaller than the monomer of the major sialoglycoprotein (periodate fuchsin sulfite 1) as judged by sodium dodecyl sulfate-polyacry lamide gel electrophoresis, and has frequently been confused with the monomer of the major sialoglycoprotein. Periodate fuchsin sulfite 2 is not labeled by the lactoperoxidase procedure in the intact cell, although it is accessible to neuraminidase and other hydrolases. On the other hand, this component can be labeled by lactoperoxidase on the cytoplasmic surface of open membranes or resealed ghosts. Thus, it is a trans membrane protein. Although most of the other transmembrane proteins of the human erythrocyte membrane are extracted from the membrane by 0.1% Triton X-100 in 7 m m phosphate buffer, pH 7.4, this component is not removed and may be a cytoskeletal component. Trypsin, chymotrypsin, and thermolysin peptides, as well as cyanogen bromide fragments, clearly indicate that the primary sequence of this polypeptide can be distinguished from dimeric or monomeric forms of the major sialoglycoprotein (periodate fuchsin sulfite 1). |
| Databáze: | OpenAIRE |
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