Purification of Murine and Feline Type-C Virus Envelope Polypeptides as Micellar Protein Complexes

Josef Schneider 1 , Heinz Falk 2 ,  and Gerhard Hunsmann 1
  • 1 Forschergruppe Tumorimmunologie, Stefan-Meier-Str. 8, D-7800 Freiburg
  • 2 Lehrstuhl für Zellbiologie der U niversität Freiburg

A technique originally described for the isolation of Friend leukaemia virus envelope polypeptides [1] yields equivalent structures from Moloney leukaemia, AKR and BALB/c xenotropic virus as well as feline leukaemia virus. The envelope polypeptides are obtained as micellar protein complexes, named rosettes. Rosettes of the five m am malian type-C viruses examined are indistinguishable by electron microscopy. Separation of these aggregates in polyacrylamide gel electrophoresis under nonreducing conditions reveals a glycoprotein of about 85 000 d as their major component. Tryptic peptide analyses identify the viral origin of these polypeptides and emphasize strain specific differences in their primary structure

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A Journal of Biosciences: Zeitschrift für Naturforschung C (ZNC) is an international scientific journal for the emerging field of natural and natural-like products. ZNC publishes original research on the isolation, bio-chemical synthesis and bioactivities of natural products, their biochemistry, pharmacology, biotechnology, and biological activity and innovative developed computational methods for predicting their structure and/or function.