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Abstract
Horse anti-human lymphocyte globulin (ALG) solutions contain, like human gamma-globulin preparations, a varying amount of IgG aggregates, which increase during longer periods of storage. Aggregate formation does not impair the immunosuppressive potency of ALG, as has been shown by prolongation of skin allograft survival time in primates. Deaggregated ALG, which can be obtained by ultracentrifugation at 100,000 g over 2 h, is less immunogenic than aggregate containing ALG. The clinical compatibility of ALG was significantly improved by ultracentrifugal deaggregation.
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