LUMINESCENCE AND PECULIARITIES OF THE STRUCTURAL STATE OF CELL PROTEINS
Abstract
On the basis of an investigation of the spectra of ultraviolet fluorescence of various tissues and organs of a frog an assumption is made concerning the very hydrophobic nature of the micro-environment around the majority of triptophane residues of cell proteins, which is explained by the absence in the cells of significant quantities of proteins whose surface contacts with the aqueous medium. Differences are revealed in the processes of denaturation of proteins with detergent (0.4% sodium dodecylsulfate; pH 3.0) in solution and in the cell, in the latter case resulting in the formation of a 'superhydrophobic' conformation of protein. By means of spectral luminescence and ATP-ase activity measurements recordings were made of conformation transitions in myofibrillar proteins under conditions of the cell and in solution under the effect of various concentrations of urea. The structural organization of the cell protects myosin from the denaturing effect of its solutions, which is manifested in the complete preservation of ATP-ase activity of cell myosin in 1 M urea and in residual activity in 8 M urea.
Document Details
- Document Type
- Technical Report
- Publication Date
- Oct 02, 1969
- Accession Number
- AD0695578
Entities
People
- S. V. Konev
- Ye. A. Chernitskiy
- Ye. I. Lin
Organizations
- United States Army Biological Warfare Laboratories