Marcozzi G
Department of Basic and Applied Biology, University of L'Aquila, Italy.
Biomed Chromatogr. 1996 Mar-Apr;10(2):97-8. doi: 10.1002/(SICI)1099-0801(199603)10:2<97::AID-BMC558>3.0.CO;2-8.
An improvement to the purification method for human salivary peroxidase is presented. The enzyme is obtained at a higher degree of purity in two chromatographic steps instead of four, and avoiding lyophilation treatment. Differences in electrophoretic pattern confirm the genetic polymorphism of the peroxidase of human saliva.
本文提出了一种人类唾液过氧化物酶纯化方法的改进。通过两个色谱步骤而非四个步骤,且避免冻干处理,可获得更高纯度的该酶。电泳图谱的差异证实了人类唾液过氧化物酶的遗传多态性。