Abstract
Summary
The mechanism of enhanced interaction of T-L with SRBC-A has been explored and the following results obtained: (1) Compared with SRBC, SRBC-A contain identical quantities of protein, phos-pholipid, and sialic acid, but have slightly reduced SH content; (2) treatment of SRBC with thiols having charge properties different from AET also facilitates rosetting; (3) exposure of SRBC to various SH-alkylating reagents, either before or after thiol treatment, does not diminish thiol-enhanced rosetting; (4) trypsinization of SRBC and of SRBC-A completely abolishes the ability of these cells to rosette; and (5) no differences could be detected between intact SRBC and SRBC-A, or in their solubilized membrane components, by SDS-PAGE and by ESR. These results indicate that free SH groups of SRBC membranes are not directly involved in the rosetting process. Thiol-enhanced rosetting probably results from cleavage of membrane S-S bridges resulting in configu-rational changes within the SRBC membrane. The interaction of an SRBC membrane receptor, probably glycoprotein in nature, with T-L is thereby facilitated.
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