Autor: |
Guliako AA, Kharitonenkov IG, Zhuravlev AI |
Jazyk: |
ruština |
Zdroj: |
Molekuliarnaia genetika, mikrobiologiia i virusologiia [Mol Gen Mikrobiol Virusol] 1986 Dec (12), pp. 40-4. |
Abstrakt: |
The accessibility and localization of tryptophane residues in the influenza viral hemagglutinin molecule have been determined by measuring specific quenching of tryptophane fluorescence by neutral (acrylamide), anionic (I-) and cationic (Cs+) quenchers. It has been shown that acrylamide quenches 64% of tryptophane fluorescence in H3-hemagglutinin whereas I- and Cs+ quench only 34%. The tryptophanyl residues have been assumed to be located in the hemagglutinin molecule both in the cationic and anionic environments. 64% of tryptophanyls have been shown to be located on the surface of the protein globule. |
Databáze: |
MEDLINE |
Externí odkaz: |
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