Abstract
Abstract The three major classes of immunoglobulins which occur in human serum (IgM, IgG and IgA) exist either singly or as multimers of 7S subunits linked together by disulfide bonds. Reductive depolymerization of these immunoglobulins ultimately results in the production of the class specific heavy chains and either kappa or lambda light chains. Papain hydrolysis of IgG results in the formation of two Fab fragments consisting of a light chain and part of a heavy chain and an Fc fragment containing the remainder of the heavy chain (1). Essentially the same results have been reported for papain hydrolysis of IgM, but the yield of the Fc fragment is very low (2). Various other proteolytic enzymes have likewise been shown to produce rather characteristic fragments of immunoglobulins (3). Recently the production of Fab and Fc fragments by reductive cleavage of human IgM and IgA with sodium borohydride has been reported (4, 5).
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
