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. 1990 Nov;64(11):5674–5677. doi: 10.1128/jvi.64.11.5674-5677.1990

Oligomeric organization of gp120 on infectious human immunodeficiency virus type 1 particles.

C D Weiss 1, J A Levy 1, J M White 1
PMCID: PMC248628  PMID: 2214033

Abstract

The oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein (gp120) was examined by treating infectious virions with chemical cross-linking agents and subjecting the protein to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and velocity centrifugation. Immunoblots of cross-linked samples revealed three gp120 bands and an approximately threefold shift in gp120 sedimentation. Our finding of cross-linking solely between gp120 suggests that the gp120 subunits are closely associated in the native envelope structure.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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