Velocity spectra of evaporation residues produced in reactions with reverse kinematics have been measured inclusively and in coincidence with charged light particles. The results indicate that the residues due to incomplete-fusion reactions originate from cluster transfer reactions with distinct Q-values and with angular momenta in the entrance channel less than the critical angular momentum l~r for complete fusion. No significant dependence on the target structure is observed.
Clusterin, a 70-Kd disulfide-linked two-chain plasma glycoprotein circulates in blood as a high-density lipoprotein particle and is highly induced after tissue injury and tissue remodeling. In this study, peripheral blood leukocytes were assayed for clusterin expression. The protein was predominantly detectable in human platelets by immune cytochemistry. The content of clusterin was determined and amounts to 2.5 +/- 1.3 micrograms/10(9) platelets, thus representing about 2% of the blood pool. Clusterin purified from human platelets had the same molecular weight as plasma clusterin under nonreducing conditions and was composed of two disulfide-linked nonidentical subunits of the same size. Both preparations were sensitive to reduction yielding the two subunits of 35 Kd. In contrast to plasma clusterin, the platelet form was not complexed to apolipoprotein A-I. By immunogold labeling, alpha-granule localization of clusterin was observed. Complete release of platelet clusterin occurred at optimal doses of A23187, phorbol myristate acetate (PMA), and thrombin. Because clusterin mRNA was detected by hybridization in situ in bone marrow- derived megakaryocytes, platelet clusterin is most likely produced and packaged into alpha-granules during megakaryocyte development.
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