It is shown that enterovirus receptors are found mainly in the microsomal fraction of disrupted primate cells. Greater virus adsorption was exhibited by disrupted cells than by intact cells, indicating that enterovinis receptor may be present on intracellular membranes as well as on the surface of the cell. Polio-virus receptor is an integral part of, or is firmly attached to, the insoluble lipoproteins of the cell. All attempts to solubilize receptor have either destroyed virus-adsorbing activity, or have failed to separate it from sedimentable lipoproteins. The destruction of poliovirus receptor activity by proteolytic enzymes, surface active agents, organic solvents, concentrated urea solutions, phenol, formaldehyde, etc., all strongly indicate that this receptor function depends upon integrity of a protein portion of the membrane lipoproteins.

This content is only available as a PDF.