Premium
Purification and Characterization of a Novel Brain‐Specific 14‐kDa Protein
Author(s) -
Nakajo Shigeo,
Omata Kumiko,
Aiuchi Toshihiro,
Shibayama Toshiko,
Okahashi Ikuko,
Ochiai Hidehiko,
Nakai Yasumitsu,
Nakaya Kazuyasu,
Nakamura Yasuharu
Publication year - 1990
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.1471-4159.1990.tb05792.x
Subject(s) - ouchterlony double immunodiffusion , sodium dodecyl sulfate , gel electrophoresis , immunocytochemistry , biochemistry , polyacrylamide gel electrophoresis , microbiology and biotechnology , amino acid , molecular mass , biology , percoll , immunodiffusion , sialoglycoprotein , chemistry , antiserum , antibody , glycoprotein , centrifugation , enzyme , immunology , endocrinology
A new acidic protein specifically present in the brain was purified to homogeneity from bovine brain. The apparent molecular mass was estimated to be 14 kDa by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, and 57 kDa by gel filtration, a finding suggesting that it exists as a tetramer under physiological conditions. The protein had a high content of Glu and Pro, and its pI was 4.3. The first six amino acid residues of the protein were Met‐Asp‐Val‐Phe‐Met‐Lys, and the amino terminal was blocked. The distribution of the protein examined by Ouchterlony gel immunodiffusion indicates that it is present specifically in brain, including rat, human, and bovine, but could not be detected in 10 other rat tissues examined. The protein was absent in Purkinje cell bodies, as examined by electron microscopic immunocyto‐chemistry, but was present in nerve terminals that make synapse‐like contacts with Purkinje cells and in neurons with dark granules in the globus pallidus of the rat.