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Proceedings Paper

Intramolecular dynamics of structure of alkaline phosphatase from Escherichia coli
Author(s): Vladimir M. Mazhul; Igor V. Mjakinnik; Alena N. Volkova
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Paper Abstract

The luminescent analysis with nano- and millisecond time resolution of intramolecular dynamics of Escherichia coli alkaline phosphatase was carried out. The effect of pH within the range 7.2 - 9.0, thermal inactivation, limited proteolysis by trypsin, binding of pyrophosphate, interconversion of enzyme and apoenzyme, the replacement of Zn2+ and Mg2+ in the active site by Cd2+ and Ni2+ on the spectral and kinetic parameters of luminescence was investigated. The essential changes of the level of nano- and millisecond dynamics of protein structure were found to correlate with the shift of enzymatic activity. The importance of small- and large-scale flexibility of protein structure for the act of enzymatic catalysis realization was shown.

Paper Details

Date Published: 2 January 1995
PDF: 5 pages
Proc. SPIE 2370, 5th International Conference on Laser Applications in Life Sciences, (2 January 1995); doi: 10.1117/12.197414
Show Author Affiliations
Vladimir M. Mazhul, Institute of Photobiology (Belarus)
Igor V. Mjakinnik, Institute of Photobiology (Belarus)
Alena N. Volkova, Institute of Photobiology (Belarus)


Published in SPIE Proceedings Vol. 2370:
5th International Conference on Laser Applications in Life Sciences

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