1.
Biochem Biophys Res Commun
; 171(1): 60-6, 1990 Aug 31.
Artículo
en Inglés
| MEDLINE
| ID: mdl-2203350
RESUMEN
A procedure is described which employs pepstatin-agarose for the affinity purification of either HIV-1 or HIV-2 protease from two similar recombinant E. coli constructs that were developed for the expression of these enzymes. HIV-2 protease was routinely expressed at much higher levels than the HIV-1 enzyme and pepstatin-agarose was the only chromatography step required to isolate pure HIV-2 protease from crude bacterial lysates. A Mono S ionic exchange step following pepstatin-agarose chromatography was sufficient to bring the HIV-1 protease to homogeneity. Purification of either enzyme can be completed in several days yielding homogeneous preparations suitable for crystallization and other physical characterization.
Asunto(s)
Endopeptidasas/aislamiento & purificación , Productos del Gen pol/aislamiento & purificación , VIH-1/enzimología , VIH-2/enzimología , Cromatografía de Afinidad , Endopeptidasas/genética , Escherichia coli , Productos del Gen pol/genética , Proteasa del VIH , Peso Molecular , Pepstatinas , Proteínas Recombinantes/aislamiento & purificación
2.
Minerva Anestesiol
; 57(9): 546-7, 1991 Sep.
Artículo
en Italiano
| MEDLINE
| ID: mdl-1798477
Asunto(s)
Anestesia , Propofol/administración & dosificación , Factores de Edad , Femenino , Humanos , Masculino , Persona de Mediana Edad
3.
Minerva Anestesiol
; 56(9): 703-5, 1990 Sep.
Artículo
en Italiano
| MEDLINE
| ID: mdl-2274168
4.
Minerva Anestesiol
; 56(7-8): 386-8, 1990.
Artículo
en Italiano
| MEDLINE
| ID: mdl-2287415