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Rat Brain α‐Mannosidase: Purification, Properties, and Interaction with Its Antibodies
Author(s) -
Zanetta J. P.,
Meyer A.,
Dontenwill M.,
Basset P.,
Vincendon G.
Publication year - 1982
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.1471-4159.1982.tb07993.x
Subject(s) - isoelectric focusing , mannosidase , isozyme , pi , isoelectric point , enzyme , biochemistry , chemistry , disulfide bond , antibody , specific activity , molecular mass , microbiology and biotechnology , biology , immunology
α ‐ d ‐Mannosidase (EC 3.2.1.24.) was purified to homogeneity from adult rat brain. The enzyme, of apparent molecular weight 397,000, appears to be formed of subunits of molecular weight 120,000 made of two protomers (62,000) bound by disulfide bridges. Isoelectric focusing gives two bands, of pi 5.40 and 5.15. Both isoenzymes seem to have the same pH curve (a small peak of activity at pH 4.5 and a maximum of activity around pH 6.0). These two isoenzymes are immunologically related.