Purification of β-N-Acetylhexosaminidase from Egg White and the Microsomal and Lysosomal Fractions of Hen Oviduct
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概要
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β-N-Acetylhexosaminidase (NAHase) was purified from egg white and the lysosomal and microsomal fractions of hen oviduct. The purification procedure included affinity chromatography using Sepharose 4B coupled with IgG specific for NAHase of hen oviduct. The isoelectric points of the three enzymes were different, but their antigen determinants were identical. In sodium dodecyl sulfate polyacrylamide gel electrophoresis, both the egg white and lysosomal enzyme gave only one protein band each, corresponding to a MW of 68000 and 53000, respectively, but the microsomal enzyme gave two protein bands, corresponding to those of the lysosomal and egg white enzymes.
- 社団法人 日本農芸化学会の論文
著者
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Ogawa Yuji
Department Of Applied Bioorganic Chemistry Gifu University
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Nakamura Ryo
Department Of Applied Biological Sciences School Of Agricultural Science Nagoya University
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Sato Yasushi
Department Of Agricultural Chemistry Meijo University
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SATO Yasushi
Department of Food Science and Technology, Nagoya University
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