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001-es BibID:	BIBFORM065370
Első szerző:	Csákó György
Cím:	Pulsed-field gel electrophoresis for the separation of large protein molecules exemplified by the isoforms of apolipoprotein (a) / Gyorgy Csako, Balint Nagy, Rene Costello, John C. Castelli, Andrew M. Hruszkewycz
Dátum:	1994
ISSN:	0173-0835
Megjegyzések:	The performance of pulsed-field gel electrophoresis (PFGE) was assessed for the separation of protein molecules. The allelic isoforms of apolipoprotein (a) (apo[a]) served as a model for this study because apo(a) is an unusually large protein, consisting of a variable number of repeating units. PFGE and, for comparison, conventional electrophoresis of human sera were carried out under reducing conditions in agarose gel. After blotting proteins onto nitrocellulose membrane, a combination of monospecific rabbit anti-apo(a) antibody and alkaline phosphatase-conjugated protein A detected apo(a) isoforms in all sera tested. The various apo(a) isoforms were effectively resolved within two repeating units ("kringles") by both PFGE and conventional electrophoresis, but the type of agarose gel used greatly affected the speed of electrophoretic separation. In a series of 89 human sera, 59 double-band and 30 single-band patterns were seen using either electrophoretic system. However, one specimen produced double bands with PFGE, while only a single band could be detected by conventional electrophoresis, and with another specimen the opposite occurred. A total of 22 different apo(a) isoforms were identified among these patterns. It is concluded that the increasingly available PFGE technology is a practical alternative to conventional agarose electrophoresis for the separation of large protein molecules.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban apolipoprotein(a) separation isoforms pulsed-field
Megjelenés:	Electrophoresis. - 15 (1994), p. 926-929. -
További szerzők:	Nagy Bálint (1956-) (molekuláris genetikus) Costello, Rene Castelli, John C. Hruskewycz, Andrew M.
Internet cím:	Szerző által megadott URL Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM065368
Első szerző:	Nagy Bálint (molekuláris genetikus)
Cím:	Downward Blotting of Proteins in a Model Based on Apolipoprotein(a) Phenotyping / Nagy Balint, Costello Rene, Csako Gyorgy
Dátum:	1995
ISSN:	0003-2697
Megjegyzések:	Standard immunoblotting ("Western blot") involves electrotransfer of proteins from a separation gel (usually acrylamide) onto a membrane. Recently, a downward capillary method with increased hybridization efficiency was developed for DNA and RNA. The present work assessed the applicability of this method to proteins in a model based on human apolipoprotein(a)[apo(a)] isoforms which consist of a single, >200-kDa polypeptide chain varying in size with a repeat sequence. After reduction treatment and sodium dodecyl sulfate-agarose gel electrophoresis, serum proteins were transferred from the gel by upward or downward (Turboblotter) capillary action onto nitrocellulose membranes in Tris-buffered saline, pH 7.5, at room temperature. Increased detectability of apo(a) isoforms was achieved by substituting comparatively high molar concentrations of protein A for true second antibody. With downward capillary transfer and short 37 degrees C incubations, the apo(a) phenotyping could be completed in about 26 h and required less than 8 h effective processing time. The downward transfer was about twice as fast (complete within 1 h) as the upward version and with this speed it offers a good alternative to electroblotting as well.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban downward blotting apolipoprotein(A) phenotyping
Megjelenés:	Analytical Biochemistry. - 231 : 1 (1995), p. 40-45. -
További szerzők:	Costello, Rene Csákó György
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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