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The acetylcholine receptor protein from human muscle was extracted with the non-ionic detergent Triton X-100 and purified by affinity chromatography on alpha-Naja toxin sepharose 4B. Further purification on Dicap-MP sepharose 4B, a choline analog compound, led to ACHR preparations with specific activities of 2-7 nmol/mg protein. The isolated receptor, labeled with 125I-alpha-bungarotoxin was characterized by different methods and compared to ACHRs from Torpedo californica electroplax and rat-denervated skeletal muscle. Gel filtration on Ultrogel AcA 34 resulted in a stokes radius of 70 A for the receptor monomer and 99 A for the dimeric form. Sucrose density gradient centrifugation showed sedimentation coefficients of 9.1 S and 13.5 S. From these data the molecular weight of the ACHR monomer was estimated as 254 000 D and 540 000 D for the receptor dimer. The isoelectric point of the 125I-alpha-bgt-ACHR complex was determined by thin-layer isoelectric focussing to be pH 5. Purified ACHRs were used for immunization of rats and mice which developed an EAMG as verified by clinical observation and electrophysical measurements. Sera from the immunized animals as well as from myasthenia gravis patients were subsequently used to compare the cross-reactivity of ACHR preparations from different sources. While antibodies of rats immunized with Torpedo ACHRs cross-reacted with ACHR preparations from rat and human skeletal muscle, antibodies from mice immunized with rat ACHR only reacted with preparations from rats and mice. Antibodies from mice immunized with ACHR of human origin exhibited a broad cross-reactivity, as did antibodies from MG patients.
I Kalies, and
F Heinz, and
R Hohlfeld, and
H Wekerle, and
K L Birnberger, and
J R Kalden
October 1995,
The European journal of neuroscience,
I Kalies, and
F Heinz, and
R Hohlfeld, and
H Wekerle, and
K L Birnberger, and
J R Kalden
October 1986,
Experimental cell research,
I Kalies, and
F Heinz, and
R Hohlfeld, and
H Wekerle, and
K L Birnberger, and
J R Kalden
May 2012,
The Journal of physiology,
I Kalies, and
F Heinz, and
R Hohlfeld, and
H Wekerle, and
K L Birnberger, and
J R Kalden
December 2011,
Proceedings of the National Academy of Sciences of the United States of America,
I Kalies, and
F Heinz, and
R Hohlfeld, and
H Wekerle, and
K L Birnberger, and
J R Kalden
January 1976,
Journal of supramolecular structure,
I Kalies, and
F Heinz, and
R Hohlfeld, and
H Wekerle, and
K L Birnberger, and
J R Kalden
September 1980,
Journal of the neurological sciences,
I Kalies, and
F Heinz, and
R Hohlfeld, and
H Wekerle, and
K L Birnberger, and
J R Kalden
November 1977,
Neurology,
I Kalies, and
F Heinz, and
R Hohlfeld, and
H Wekerle, and
K L Birnberger, and
J R Kalden
March 2016,
Proceedings of the National Academy of Sciences of the United States of America,
I Kalies, and
F Heinz, and
R Hohlfeld, and
H Wekerle, and
K L Birnberger, and
J R Kalden
December 1988,
The Journal of biological chemistry,
I Kalies, and
F Heinz, and
R Hohlfeld, and
H Wekerle, and
K L Birnberger, and
J R Kalden
January 1981,
Scandinavian journal of immunology,
