Isolation, Purification, and Characterization of an Acidic Rrotein in the Cerebrospinal Fluid of Central Nervous System Disease
スポンサーリンク
概要
- 論文の詳細を見る
Proteins from 21 cerebrospinal fluid (CSF) samples (14 derived from neurological cases and 7 from normal individuals) and 15 serum samples (11 from neurological cases and 4 from normal individuals) were analyzed by two-dimensional electrophoresis. Protein mapping revealed a very acidic protein (Ac-P) at about pH 3.5 in the 71% of CSF samples from neurological cases. However, no serum sample contained Ac-P. Ac-P was isolated and purified, and determined to be a glycoprotein containing a large amount of carbohydrate, with molecular weight 42,000 and isoelectric point 2.7-3.3. The amino acid composition of Ac-P was consistent with α_1-acid glycoprotein (AGP), and Ac-P was responsive to a commercial anti-AGP antiserum in the radial immunodiffusion test. The known polymorphism of AGP suggests some differences in physicochemical properties such as molecular weight and isoelectric point between AGP in serum and in CSF. Quantitative analysis of Ac-P (AGP) and total protein levels in CSF showed a partial interdependence. Ac-P may be a useful marker for detecting a pathological conditions of the central nervous system.
- 日本脳神経外科学会の論文
- 1992-10-15
著者
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FUKUSHIMA Yoshiharu
Department of Neurosurgery,School of Medicine,Tokyo Medical
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Fukushima Yoshiharu
Department Of Neurosurgery Fujigaoka Hospital Showa University
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ASAI Jun-ichiro
Department of Neurosurgery, Fujigaoka Hospital, Showa University
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MAKINO Yoshiaki
First Department of Biochemistry, Showa University School of Medicine
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Makino Yoshiaki
First Department Of Biochemistry Showa University School Of Medicine
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Asai Jun-ichiro
Department Of Neurosurgery Fujigaoka Hospital Showa University
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Fukushima Yoshiharu
Department Of Neurosurgery Faculty Of Medicine Tokyo Medical:dental University
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