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HUMAN BRAIN‐SPECIFIC ALPHA 2 ‐GLYCOPROTEIN: PURIFICATION BY AFFINITY CHROMATOGRAPHY AND DETECTION OF A NEW COMPONENT; LOCALIZATION IN NERVOUS CELLS 1
Author(s) -
Warecka Krystyna,
Møller H. J.,
Vogel H.M.,
Tripatzis I.
Publication year - 1972
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.1471-4159.1972.tb01387.x
Subject(s) - neuropil , human brain , affinity chromatography , glycoprotein , centrifugation , alpha (finance) , biology , sepharose , central nervous system , biochemistry , chemistry , microbiology and biotechnology , enzyme , neuroscience , medicine , construct validity , nursing , patient satisfaction
— Human brain‐specific alpha 2 ‐glycoprotein was purified by means of Sepharose immunoadsorbents. A further brain‐specific protein was found by this method. This component appears to be present in brain in low concentrations only and has been enriched by affinity chromatography. Glial cells of human brain were separated from neurons by a density centrifugation method and four fractions were obtained: neuropil, neuronal perikarya, nuclei and debris. Each fraction was checked by light and phase contrast microscopy to estimate the intactness of the cells and any contamination by other fractions, and also immunologically for determination of brain‐specific alpha 2 ‐glyco‐protein. The results indicate that localization of this brain‐specific protein is in the cyto‐plasm of the glial cells. The results are discussed in terms of a possible role of this protein in the inflammatory response and in some demyelinating diseases.