Premium
A Procedure for Preparing Immunoglobulin G from Human and Monkey Blood
Author(s) -
Sgouris James T.,
Storey Ralph W.,
Wolfe Richard W.,
Anderson George R.
Publication year - 1966
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1111/j.1537-2995.1966.tb04713.x
Subject(s) - antibody , antiserum , immunoelectrophoresis , chromatography , chemistry , electrophoresis , immunoglobulin g , microbiology and biotechnology , biology , immunology
Immunoglobulin G was prepared from human plasma and monkey serum containing demonstrable titers of tetanus, diphtheria and rabies antibodies by a batchwise technic using diethylaminoethyl cellulose (DEAE). The preparation was comparable to that prepared by the cold ethanol technic of Oncley et al. Moving boundary electrophoresis (Tiselius) of the DEAE immunoglobulin preparations revealed that the human IgG had a purity of 98.5 per cent and the monkey IgG of 99.5 per cent (i.e., mobilities less than 2.8 × 10 −5 /cm 2 /V/sec) comparable to the cold ethanol preparations. Vertical starch gel electrophoresis (Smithies) revealed that both preparations consisted of one broad band. Immunoelectrophoretic studies, using anti‐human horse or goat sera, confirmed the observation that only one component was present in the final preparations. Disc electrophoresis revealed one broad band plus a faster minor component. When immunoglobulin G, M and A antisera were utilized in Immunoelectrophoresis, these preparations reacted only with the IgG antisera. The concentration of tetanus, diphtheria and rabies antibodies by the DEAE method was comparable to the cold ethanol preparations.