Biophysical and biochemical characterization of lymphocytic choriomeningitis virus

Autor:	Kenneth P. Camyre, C. J. Pfau
Rok vydání:	1967
Předmět:	Tris Infectivity Chromatography biology Hydrochloride viruses Sonication General Medicine Lymphocytic choriomeningitis medicine.disease Virology Virus chemistry.chemical_compound chemistry medicine biology.protein Hydroxymethyl Bovine serum albumin
Zdroj:	Archiv f�r die gesamte Virusforschung. 20:430-437
ISSN:	1432-8798 0304-8608
Popis:	The infectivity of LCM virus suspended in solutions buffered with Tris(hydroxymethyl)aminomethane and its hydrochloride has been found to be greatly stabilized. This stabilization (studied at 4° and 37° C), however, was markedly dependent on the protein content of the solution. If the protein content became too low (by dilution and/or partial purification of the virus), the Tris effect would disappear, but could be reversed if bovine serum albumin was added before inactivation studies were begun. The sensitivity of the virus to ultrasonic irradiation also followed the pattern established above (i.e. — diluted or purified virus was inactivated to a much greater extent than virus suspended in Eagle's medium plus serum). The data also indicated that sonication could break up aggregates of virus particles.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::56ea42a3baf2f21e780592c74e8b5577 https://doi.org/10.1007/bf01275223 Zobrazit plný text záznamu Full text from SpringerLink