Separation of univalent fragments from the bivalent rabbit antibody molecule by reduction of disulfide bonds

Studies of anti‐f(ab')2 antibodies and possible immunologic control mechanisms in systemic lupus erythematosus

“…Human IgG was obtained by DEAE-cellulose chromatography of Cohn fraction I1 (Sigma), using 0.015M sodium phosphate buffer, pH 6.3. Normal human F(ab')z was prepared according to the method of Nisonoff et al, with slight modification (2% pepsin digestion in acetate buffer, pH 4.1) (31). F(ab')ranti-DNA was prepared from isolated anti-DNA antibodies ob-tained from 2 different SLE patients during periods of active disease.…”

The action of pepsin on protein fractions from horse antisera to diphtheria toxin

“…Nisonoff, Wissler, Lipman & Woernley (1960) have shown that pepsin, acting on rabbit y-globulin antibody at pH 4-5, decreases the molecular weight from 160 000 to 100 000. This smaller molecule still precipitates specifically with its homologous antigen, but can be further split into two parts by reagents capable ofreducing disulphide bonds.…”

Phosphorylation of NADPH‐cytochrome c reductase in guinea pig peritoneal macrophages stimulated with phorbol myristate acetate

“…Guinea pig anti-ovalbumin antibody was also specifically purified as described in 1181. The F(ab')zs of these antibodies were prepared by pepsin digestion [18,19] and conjugated to CNBr-activated Sepharose CL-4B (Pharmacia) [20]. Protein kinase C was partially purified from guinea pig brain by the first step of the procedure described by Inagaki et al [21].…”