ALTERATION IN THE ELECTROPHORETIC MOBILITY OF OMPC DUE TO VARIATIONS IN THE AMMONIUM PERSULFATE CONCENTRATION IN SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL-ELECTROPHORESIS

Author	dc.contributor.author	Lobos, S.
Author	dc.contributor.author	Mora, Guido C.	es_CL
Admission date	dc.date.accessioned	2011-04-21T19:09:05Z
Available date	dc.date.available	2011-04-21T19:09:05Z
Publication date	dc.date.issued	1991-06
Cita de ítem	dc.identifier.citation	ELECTROPHORESIS 12 (6): 448-450	es_CL
Identifier	dc.identifier.issn	0173-0835
Identifier	dc.identifier.uri	https://repositorio.uchile.cl/handle/2250/121185
Abstract	dc.description.abstract	Studies on Salmonella typhi and Salmonella typhimurium outer membrane proteins have shown that the relative position of OmpC porin in sodium dodecyl sulfate-polyacrylamide gel electrophoresis undergoes an important shift when the concentration of ammonium persulfate in the running gel is increased from 6 to 12 mm. The apparent molecular mass at these concentrations was estimated to be 34 and 40 kDa, respectively. Under similar electrophoretic conditions the apparent molecular mass estimated for OmpF was 37.6 and 38.2 kDa. Therefore, OmpC moves from a leading position to a position behind OmpF. For Escherichia coli OmpC the shift observed is less pronounced than that occurring in Salmonellae.	es_CL
Lenguage	dc.language.iso	en	es_CL
Publisher	dc.publisher	VCH PUBLISHERS INC	es_CL
Keywords	dc.subject	HEAT-MODIFIABLE PROTEIN	es_CL
Título	dc.title	ALTERATION IN THE ELECTROPHORETIC MOBILITY OF OMPC DUE TO VARIATIONS IN THE AMMONIUM PERSULFATE CONCENTRATION IN SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL-ELECTROPHORESIS	es_CL
Document type	dc.type	Artículo de revista