[Conjugation of bovine gammaglobulin to L-asparaginase (E. coli) (author's transl)].
Bovine gammaglobulin-L-asparaginase conjugates were prepared with an enzymic activity of about 30 IU/mg. Glutardialdehyde was used as bifunctional reagent for the cross-linking in an optimal concentration of 0.16 mg/10 mg protein. The both components were found in the conjugates in a ratio of 1:1.5. The recovery was about 25% of the initial protein amounts. The antigenic specificity of the globulin component decreased up to 60%, the enzymic activity also up to 60% by the conjugation.
D000818:Animals; D001215:Asparaginase / Q000378:metabolism*; D002417:Cattle; D004926:Escherichia coli / Q000201:enzymology; D005976:Glutaral; D007166:Immunosuppressive Agents; D011485:Protein Binding; D005719:gamma-Globulins / Q000378:metabolism*
D007166:Immunosuppressive Agents; D005719:gamma-Globulins; D001215:Asparaginase; D005976:Glutaral
Konjugation von Rindergammaglobulin an L-Asparaginase (E. coli).