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ELECTROPHORETIC ANALYSIS OF THE HIGHLY BASIC PROTEINS OF THE RAT BRAIN FRACTION WHICH INDUCES EXPERIMENTAL ALLERGIC ENCEPHALOMYELITIS
Author(s) -
Martenson R. E.,
Gaitonde M. K.
Publication year - 1969
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1969.tb10372.x
Subject(s) - major basic protein , myelin basic protein , isoelectric point , encephalomyelitis , electrophoresis , myelin , polyacrylamide gel electrophoresis , isoelectric focusing , biochemistry , staining , gel electrophoresis , chromatography , urea , biology , chemistry , microbiology and biotechnology , immunology , central nervous system , enzyme , multiple sclerosis , endocrinology , genetics , eosinophil , asthma
— A purified basic protein fraction of adult rat brain when injected into guinea pigs induced experimental allergic encephalomyelitis (EAE). The freeze‐dried preparations were subjected to electrophoresis on 5% polyacrylamide gel at pH 10.6 in the presence of 8 m ‐urea to obtain one‐step separation of highly basic proteins from other proteins. Under these conditions the highly basic proteins whose isoelectric point exceeded pH 10.0 gave seven distinct components. After staining these protein bands with naphthalene black 10B they were scanned densitometrically: the area under each peak was computed and used for calculation of the amounts of individual basic proteins. The acid extracts of rat brain contained 2.61–3.95 mg highly basic proteins/g fresh tissue. A comparison of the electrophoretic patterns of acid extracts of rat brain and liver showed that two of the highly basic proteins (components 1 and 2) were present only in the brain and not in the liver. These two components in the brain were attributed to proteins of the myelin sheath.