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Asian Journal of Biochemistry

Year: 2006 | Volume: 1 | Issue: 2 | Page No.: 153-161
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Authors

Bijan Ranjbar

Saied Afshar

Ali Kakanejadifard

Khosro Khajeh

Hossein Naderi-Manesh

Leila Hassani

Naader Alizadeh

Keywords

Kinetic and structural studies have been made on the effect of glyoxime (GO) and dichloroglyoxime (DCGO) on the activity and the structure of lysozyme in 100 mM potassium phosphate buffer, pH 7.0, using UV spectrophotometry, circular dichroism (CD) and fluorescence spectroscopy techniques. GO and DCGO act as an uncompetitive inhibitors with Ki = 99 and 52 µM, respectively. Circular dichroism studies show that the secondary structure of the enzyme in the presence of different concentrations of GO and DCGO does not show considerable change. Kinetic results show that at low concentration of GO (0.12-120 µM) and DCGO (0.07-64 µM) considerable inhibition of enzyme could be seen, but the fluorescence data show that there is not noticeable change in the tertiary structure of lysozyme at low concentration of inhibitors. Also, these results indicate considerable decrease in the tertiary fold of the lysozyme at high concentrations of GO and DCGO espetially dichloroglyoxime. Results show that, lysozyme in the presence of high concentration of GO (1200 µM) and DCGO (640 µM), presents structural characteristics of a molten globule like state.
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