TY - JOUR
T1 - Affinity chromatography purification of erythrocyte membrane proteins after selective labeling with trinitrobenzene sodium sulfonate
AU - Tarone, Guido
AU - Prat, Maria
AU - Comoglio, Paolo M.
N1 - Funding Information:
We wish to thank Miss M. R. Amedeo for skilful technical assistance. This work was supported by a research contract with the Italian National Research Council (C.N.R.).
PY - 1973/6/22
Y1 - 1973/6/22
N2 - 2,4,6-Trinitrobenzene sodium sulfonate may be used, under appropriate conditions, for specific surface labeling of erythrocyte plasma membranes. Trinitrophenylated ghost proteins are easily purified by reverse immunoadsorption using rabbit anti-dinitrophenyl antibodies covalently linked to Sepharose 4B. The advantages of a method that permits selective labeling of membrane molecules with a hapten and their purification by affinity chromatography are obvious. The possible applications of such a method in the investigation of the composition of plasma membranes are discussed.
AB - 2,4,6-Trinitrobenzene sodium sulfonate may be used, under appropriate conditions, for specific surface labeling of erythrocyte plasma membranes. Trinitrophenylated ghost proteins are easily purified by reverse immunoadsorption using rabbit anti-dinitrophenyl antibodies covalently linked to Sepharose 4B. The advantages of a method that permits selective labeling of membrane molecules with a hapten and their purification by affinity chromatography are obvious. The possible applications of such a method in the investigation of the composition of plasma membranes are discussed.
UR - http://www.scopus.com/inward/record.url?scp=0015800259&partnerID=8YFLogxK
U2 - 10.1016/0005-2736(73)90268-X
DO - 10.1016/0005-2736(73)90268-X
M3 - Article
SN - 0005-2736
VL - 311
SP - 214
EP - 221
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
IS - 2
ER -