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  • Author: Josef Schneider x
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Zukunft gestalten – Bestand erhalten/Shaping the Future – Conserving the Present
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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

Room-temperature Mössbauer spectra are reported for μ3-RP-bridged heterometallic iron clusters of the type μ3-RP-(C5H5(CO)2Mn)Fe2(CO)6Ln. The Mössbauer parameters of these clusters show that the structures are in agreement with the lattice constants of low-spin hetero manganese-iron clusters

Abstract

A glycoprotein of an apparent molecular mass of 46000, gp 46, was enriched by affinity chromatography from the virus-and cell-free culture medium of adult T-cell leukemia virus (ATLV) infected cells, gp 46 was specifically precipi­tated with sera from patients with adult T-cell leukemia known to react with the adult T-cell leukemia associated antigen (ATLA). Thus, gp 46 is a novel component of the ATLA antigen complex.