The purification and characterization of a major glycoprotein of the murine mammary tumor virus

article

Westenbrink, F.

Koornstra, W.
Affinity chromatography of solubilized murine mammary tumor virus on concanavalin A-Sepharose was clearly affected by different mixtures of detergent present in the elution buffer: A complex consisting of a glycoprotein of 52,000 daltons (gp52), and a glycoprotein of 36,000 daltons (gp36), besides free gp52 were isolated. The gp36 could be purified by gel filtration of the complex in the presence of a high concentration of sodium deoxycholate. The elution of gp36 in the void volume of the Sephadex column and the results obtained with sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed strong hydrophobic interactions within the molecule. The glycoprotein was immunochemically characterized by competitive radioimmunoassay and immunoelectrophoresis. No cross-reactivity of gp36 with gp52 or two nonglycosylated viral polypeptides was observed. © 1979.
Chemicals/CAS: Epitopes; Glycoproteins; Viral Proteins
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epitopeglycoproteinvirus proteinanimalclassificationimmunoelectrophoresisimmunologyisolation and purificationmouseMouse mammary tumor oncovirusradioimmunoassayAnimalEpitopesGlycoproteinsImmunoelectrophoresisMammary Tumor Virus, MouseMiceRadioimmunoassaySupport, U.S. Gov't, P.H.S.Viral Proteins
TNO Identifier
228663
Repository link
https://resolver.tno.nl/uuid:13adbcef-32af-4fd2-92e0-c6e2c5e28a93
ISSN
0003-2697
Source
Analytical Biochemistry, 94(1), pp. 40-47.
Pages
40-47
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