A rapid and efficient method for the purification of the complement subcomponents C1r and C1s in zymogen form using fast protein chromatography.
The purification of the subcomponents C1r and C1s of the first component of complement involves multiple steps and is time-consuming. This accounts for the frequently observed partial activation of the subcomponents. In this report we propose a simplified procedure of purification using a batch method and fast protein chromatography avoiding a shift of pH. The method provides C1r and C1s in a yield of 35 and 60% respectively. In addition, this study provides a simple and sensitive test to assess functional purity of C1r and C1s with respect to the other C1 subcomponents.
Peitsch
M C
MC
Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland.
Kovacsovics
T J
TJ
Isliker
H
H
D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D003166:Complement Activating Enzymes / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D003172:Complement C1 / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D015923:Complement C1r; D003173:Complement C1s / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D003171:Complement Pathway, Classical; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans
D003172:Complement C1; D004792:Enzyme Precursors; D003166:Complement Activating Enzymes; D015923:Complement C1r; D003173:Complement C1s