ABSTRACT
Human plasma alpha-galactosidase A (alpha-D-galactoside galactohydrolase, EC 3.2.1.22) was purified 7000-fold over plasma levels from Cohn Fraction IV-1. The yield per kg starting material averaged 11 000 units (nmol galactose liberated per h) and the specific activity was about 600 units per mg protein with 4-methylumbelliferyl-alpha-D-galactoside. The ratio of 4-methylumbelliferyl-alpha-galactosidase to ceramide trihexosidase activities was 6.2. Both activities were heat labile and exhibited the same relative mobilities on polyacrylamide gel electrophoresis. Enzymatic activity was stable for at least 4 months at 4 and -20 degrees C. The endotoxin concentration of this preparation averaged 0.26 mg per mg protein.
Subject(s)
Galactosidases/blood , alpha-Galactosidase/blood , Humans , Kinetics , Temperature , alpha-Galactosidase/isolation & purificationABSTRACT
To determine the effect of fragmentation on potency of immune globulin preparations, two comparisons were carried out. In one study, the immune globulin was derived from American plasma; in the other, the source was Israeli plasma. In each of the two studies, three materials were given to household contacts of icteric hepatitis: (1) human albumin as a placebo; (2) immune globulin with the IgG intact; and (3) immune globulin of the same lot with the IgG deliberately fragmented by added fibrinolysin. Comparable reductions in secondary attack rates were achieved with fragmented and unfragmented materials from both lots. Fragmentation, therefore, had no deleterious effect. In addition, it was found that American globulin is comparable to Israeli globulin for protection against strains of Type A hepatitis prevalent in Israel. Administration in the second half (last 15 days) of the incubation period did not reduce the frequency of icteric disease.
