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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Biophysical Characterization Of An Insect Lysozyme From Manduca Sexta

Author(s): Alonso A. Lopez-Zavala, Enrique de-la-Re-Vega, Sergio A. Calderon-Arredondo, Karina D. Garcia-Orozco, Enrique F. Velazquez, Maria A. Islas-Osuna, Miguel A. Valdez and Rogerio R. Sotelo-Mundo

Volume 11 , Issue 1 , 2004

Page: [85 - 92] Pages: 8

DOI: 10.2174/0929866043478374

Price: $65

Abstract

Insect lysozyme from Manduca sexta (MS-lys) was overexpressed in E. coli and refolded to obtain active protein. Recombinant MS-lys presented a globular structure, with an alpha-helical content of 57% as assessed by circular dichroism spectroscopy. Light scattering studies showed that in solution MSlys has a quasi-monodisperse size distribution, with a rod-like structure similar to nucleation clusters reported in egg lysozyme pre-crystallization stages. These results show that MS-lys is an excellent candidate for crystallization, folding and denaturation studies.

Keywords: lysozyme, insect, manduca sexta, circular dichroism, dynamic light scattering, secondary structure


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