Bovine Liver β-Acetylhexosaminidase. Purification by Hydrophobic Affinity Chromatography and Heterogeneity
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概要
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Bovine liver β-acetylhexosaminidase A (Hex A) and B (Hex B) were purified by hydrophobic affinity chromatography. Octyl Sepharose CL-4B was more effective than Phenyl Sepharose CL-4B as an adsorbent. Both the crude and the purified preparations of Hex A and Hex B exhibited extensive heterogeneity when focused on a polyacrylamide gel plate with pH gradient ; Hex A gave at least ten bands with pI's ranging from 5.0 to 7.0,and Hex B at least fourteen bands with pI's ranging from 6.5 to 8.5. Stepwise elution with increasing pH from a CM-cellulose column resulted in rough separation of Hex A and Hex B into overlapping classes.
- 社団法人日本薬学会の論文
- 1978-10-25
著者
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村田 早苗
School of Pharmaceutical Science, Toho University
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田中 光也
School Of Pharmaceutical Sciences Toho University
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田中 光也
Faculty of Pharmaceutical Sciences, Toho University
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京坂 重久
Faculty of Pharmaceutical Sciences, Toho University
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村田 早苗
Faculty of Pharmaceutical Sciences, Toho University
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京坂 重久
School Of Pharmaceutical Sciences Toho University
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村田 早苗
School Of Pharmaceutical Science Toho University
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