Immunoglobulin bound to platelets as immune complexes or specific antibody in specimens from acquired immunodeficiency syndrome and immune thrombocytopenic purpura.

Acquired immunodeficiency syndrome (AIDS), lymphadenopathy syndrome (LAS), and immune thrombocytopenic purpura (ITP) specimens were tested by an enzyme-linked immunosorbent assay (ELISA) for immunoglobulin (Ig) bound to platelets. All specimen evaluations were performed with General Diagnostic's newly developed kit procedure. The test measured but did not distinguish immune complex (IC) binding with platelet Fc receptor sites from platelet-specific antibody (PAb) binding with platelet antigen Fab-binding sites.

Cancer therapy with chemically modified enzymes. II. The therapeutic effectiveness of arginase, and arginase modified by the covalent attachment of polyethylene glycol, on the taper liver tumor and the L5178Y murine leukemia.

Monomethoxypolyethylene glycol (PEG) was attached covalently to arginase. PEG-arginase was effective in prolonging the survival times of mice injected with the Taper liver tumor, whereas unmodified arginase was ineffective. PEG-arginase was more effective than arginase in the in vitro destruction of L5178Y mouse leukemia.

Induction of tolerance in mice by uricase and monomethoxypolyethylene glycol-modified uricase.

The ability to induce tolerance to uricase by the administration of native uricase, and uricase modified by the covalent attachment of monomethoxypolyethylene glycol (PEG) was examined. Uricase, and uricase with PEG attached to 35% (PEG-uricase 35%) and 70% (PEG-uricase 70%) of available amino groups were found to induce tolerance in mice not previously sensitized to uricase. There was a dampening of the IgG, IgE and IgM antibody response to uricase which persisted even after a second sensitizing dose of uricase was administered to these animals.

Preparation of a non-immunogenic arginase by the covalent attachment of polyethylene glycol.

Methoxypolyethylene glycol of 5000 daltons (PEG) was attached covalently to bovine liver arginase using 2,4,6-trichloro-s-triazine as the coupling agent. The conjugate (PEG-arginase), with PEG attached to 53% of the amino groups, retained 65% of its original enzymatic activity. Mice were injected intravenously with arginase or PEG-arginase for periods of one to three months.