Isolation and partial characterization of a fragment corresponding to the dimeric form of the CH2 domain of rabbit IgG.
A fragment corresponding to the intact dimeric form of the CH2 domain of rabbit IgG, including the hinge region disulfide linkage, was obtained by plasmin digestion of crystalline Fc derived from IgG by the action of papain. Identification and assessment of purity of the fragment was established by SDS-PAGE, amino acid composition analysis, N-terminus sequence and C-terminus amino acid analysis and SDS-urea-PAGE of the reduced fragment. The fragment retains serologic reactivity with anti-Fc specific antisera. Comparison of deglycosylation by endoglycosidase F indicates a more open special relationship between the two CH2 domains in the fragment than in Fc.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000494:pharmacology; D007127:Immunoglobulin Constant Regions / Q000302:isolation & purification*; D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains / Q000302:isolation & purification*; D007136:Immunoglobulins / Q000302:isolation & purification*; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D011817:Rabbits
D000596:Amino Acids; D002241:Carbohydrates; D007127:Immunoglobulin Constant Regions; D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains; D007136:Immunoglobulins; D006026:Glycoside Hydrolases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase