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A RADIOIMMUNOASSAY FOR MYELIN BASIC PROTEIN AND ITS USE FOR QUANTITATIVE MEASUREMENTS
Author(s) -
Cohen S. R.,
McKhann G. M.,
Guarnieri M.
Publication year - 1975
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.1471-4159.1975.tb04329.x
Subject(s) - myelin basic protein , radioimmunoassay , myelin , antibody , chemistry , chromatography , electrophoresis , brain tissue , biochemistry , biology , central nervous system , immunology , anatomy , endocrinology
—A specific radioimmunoassay (RIA) for myelin basic protein is described which is sensitive to 10 −9 g of basic protein. The amount of basic protein detected in isolated myelin by the RIA and by SDS‐gel electrophoresis and spectrophotometric quantitation agree to within experimental error. In contrast to isolated myelin, the major portion of the basic protein in fresh tissue is not accessible to its antibody. It is shielded from its antibody in a complex which is disrupted by heat, organic solvents, and various detergents. Maximum antibody binding was obtained with tissue heated to 100°C for 10 min. It is possible to calculate that the RIA quantitatively detects basic protein in boiled tissue. Boiled adult rat brain contains approximately 2·5 μg of basic protein/mg wet wt of cerebral cortex. The antibody to basic protein has no capacity to bind non‐neural tissues.