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绵羊肝脏β-N-乙酰己糖胺酶:部分纯化、特性鉴定及光动力灭活

Sheep liver beta-N-acetylhexosaminidase: partial purification, characterization and photodynamic inactivation.

作者信息

Donoso L A, Spikes J D

出版信息

Enzyme. 1980;25(2):111-7. doi: 10.1159/000459229.

Abstract

Sheep liver beta-N-acetylhexosaminidase was purified over 20-fold by conventional methods. The enzyme possessed activity against both p-nitrophenly-beta-D-N-acetylglucosaminide and p-nitrophenyl-beta-D-N-acetylgalactosaminide as substrates. On the basis of a variety of physical and chemical analyses including pH stability, substrate inhibition studies and photodynamic inactivation, it was concluded that both the beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase activities reside within the same molecule.

摘要

采用常规方法将羊肝β-N-乙酰己糖胺酶纯化了20多倍。该酶以对硝基苯基-β-D-N-乙酰葡糖胺和对硝基苯基-β-D-N-乙酰半乳糖胺作为底物均具有活性。基于包括pH稳定性、底物抑制研究和光动力失活在内的多种物理和化学分析,得出结论:β-N-乙酰葡糖胺酶和β-N-乙酰半乳糖胺酶活性均存在于同一分子中。

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