NMR studies of the interaction betweenBacillis subtilis neutral proteinase and inorganic metal compounds
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://link.springer.com/content/pdf/10.1007/BF02886262.pdf
Reference5 articles.
1. McConn, J. D., Tsuru, D., Yasunobu, D. T.,Bacillis subtilis neutral proteinase (I)—A zinc enzyme of high specific activity, J. Boil. Chem., 1964, 239: 3706.
2. Tsuru, D., McConn, J. D., Yasunobu, K. T.,Bacillis subtilis neutral proteinase (II)—Some physicochemical properties, J. Biol. Chem., 1965, 240: 2415.
3. Hu, J. H., Xu, Y. T., Zheng, X. F. et al., A new method of NMR technique in the study of active central structure of metalloenzyme, Chinese Science Bulletin, 1997, 42(20): 1703.
4. Giovanni, S., Claudio, V., Angelo, F. et al., Structural feature of neutral proteinase fromBacillus subtilis deduced from model-building and limited proteolysis experiments, Eur. J. Biochem., 1990, 189(2): 221.
5. Homes, M. A., Mathews, B. W., Structure of thermolysin refined at 1.67Å resolution, J. Mol. Biol., 1982, 160: 623.
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