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The agglutination of human platelets by bovine factor VIII related protein has been studied in relation to the presence or absence of the 145ooo molecular weight, soluble platelet glycoprotein (GPS) using the presence of a granule-located glycoprotein as a positive control. GPS is found in the soluble fraction after subcellular fractionation of platelet homogenates on sucrose density gradients, and is probably identical to the soluble membrane protein glycocalicin The granule and the soluble glycoproteins separate into two bands on SDS-polyacrylamide gels both in reduced and unreduced samples when the gels contain urea and EDTA and are stained with periodic acid-Schiff reagent (PAS). A concomitant loss, or specific elution, of GPS and loss of agglutination was observed when platelets were stored in Tris-buffered saline, pH 7.4 (TS)at 4°C for 7 days, or when freshly prepared platelets were frozen and thawed when suspended in TS. When suspended in an EDTA-containing buffer during freezing and thawing, the resulting platelet ghosts still contained GPS and still agglutinated. The soluble fraction obtained by subcellular fractionation of giant platelets(Bernard-Soulier)did not show any PAS bands, whereas soluble fraction of these platelets prepared by freezing and thawing in TS clearly showed the presence of the granule protein but not the GPS band. The data indicate an association between GPS and the agglutination phenomenon.

Absence of the 145000 Molecular Weight, Soluble Platelet Glycoprotein - Lack of Platelet Agglutination