Polymerization of tobacco mosaic virus protein without and with hydrogen ion binding

Autor: Ragaa A. Shalaby, Max A. Lauffer
Rok vydání: 1983
Předmět:
Zdroj: Archives of Biochemistry and Biophysics. 223:224-234
ISSN: 0003-9861
DOI: 10.1016/0003-9861(83)90588-x
Popis: When tobacco mosaic virus (TMV) protein is polymerized at pH values above 7 in unbuffered solutions, either by raising temperature at constant ionic strength or by increasing ionic strength at constant temperature, a 20 S component is formed having bound only the very small amount of H+ ion supplied by the unpolymerized protein. When hydrogen ion is added by titration during polymerization so as to keep pH constant, as would occur automatically if a buffer were present, a 20 S component is formed with one H+ ion bound each for half of the subunits. Thus, a 20 S form with and a 20 S form without bound H+ ion exist. Furthermore, the 20 S form without bound H+ ion binds H+ ion when supplied by titration to produce a 20 S form with the same amount of bound H+ ion as when H+ ion is supplied during the polymerization.
Databáze: OpenAIRE