Identification and isolation of calcium-dependent and -independent bovine immunoglobulins reactive with sepharose 4B.
Calcium-dependent and -independent Sepharose 4B-binding bovine serum proteins were isolated by affinity chromatography on unsubstituted Sepharose 4B using 2 mM ethylenediamine tetraacetic acid followed by 0.1 M galactose. They appeared in two different protein peaks by gel filtration on Sephacryl S-200. The earlier eluted protein was demonstrated to be immunologically IgM, whereas the retarded one IgG. From these findings, Sepharose 4B-binding bovine serum proteins are suggested to be calcium-dependent and -independent immunoglobulins IgM and IgG.
Sugii
S
S
Department of Serology and Immunology, School of Medical Technology, Kitasato University, Kanagawa, Japan.
Hirota
Y
Y
D000818:Animals; D001798:Blood Proteins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D002135:Calcium-Binding Proteins; D002417:Cattle; D002846:Chromatography, Affinity; D004492:Edetic Acid; D006384:Hemagglutination; D006385:Hemagglutination Inhibition Tests; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007074:Immunoglobulin G / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D007075:Immunoglobulin M / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D011485:Protein Binding; D012685:Sepharose / Q000378:metabolism
D001798:Blood Proteins; D002135:Calcium-Binding Proteins; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D012685:Sepharose; D004492:Edetic Acid