Fast and efficient separation of immunoglobulin M from immunoglobulin G using short monolithic columns.
Certain diagnostic, analytical and preparative applications require the separation of immunoglobulin G (IgG) from immunoglobulin M (IgM). In the present work, different ion-exchange methacrylate monoliths were tested for the separation of IgG and IgM. The strong anion-exchange column had the highest dynamic binding capacity reaching more than 20mg of IgM/ml of support. Additionally, separation of IgM from human serum albumin, a common contaminant in immunoglobulin purification, was achieved on the weak ethylenediamino anion-exchange column, which set the basis for the IgM purification method developed on convective interaction media (CIM) supports. Experiments also confirmed flow independent characteristics of the short monolithic columns.
Brne
P
P
BIA Separations d.o.o., Teslova 30, SI-1000 Ljubljana, Slovenia.
Podgornik
A
A
Bencina
K
K
Gabor
B
B
Strancar
A
A
Peterka
M
M
D002851:Chromatography, High Pressure Liquid / Q000295:instrumentation* / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007074:Immunoglobulin G / Q000737:chemistry / Q000302:isolation & purification*; D007075:Immunoglobulin M / Q000737:chemistry / Q000302:isolation & purification*; D015203:Reproducibility of Results; D012709:Serum Albumin / Q000737:chemistry / Q000302:isolation & purification
D007074:Immunoglobulin G; D007075:Immunoglobulin M; D012709:Serum Albumin