A soman-hydrolyzing enzyme (somanase) was purified from human liver. The human somanase is capable of hydrolyzing pinacolyl methylphosphonofluoridate (soman), diisopropylphosphorofluoridate (DFP), and ethyl-N-dimethyl phosphoramidocyanidate (Tabun) with P-F or P-CN bonding, but not ethyl (S-2-diisop
Purification and study of the physiocochemical properties of angiotensin-converting enzyme from human liver
β Scribed by I. Yu. Sakharov; S. M. Danilov; N. V. Sukhova
- Publisher
- Springer US
- Year
- 1987
- Tongue
- English
- Weight
- 240 KB
- Volume
- 103
- Category
- Article
- ISSN
- 0007-4888
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## Abstract We have cloned, over expressed, and purified one of the two catalytic domains (residues Ala^361^ to Gly^468^, ACEβN) of human somatic angiotensinβI converting enzyme in __Escherichia coli.__ This construct represents the __N__βcatalytic domain including the two binding motifs and the 23