Investigation of chromatographic performances and binding characteristics of BSA-encapsulated capillary column prepared by the sol-gel method.
We have developed a novel protein-encapsulation technique using the sol-gel method for the preparation of monolithic capillary columns for capillary electrochromatography. Bovine serum albumin (BSA) was encapsulated in tetramethoxysilane-based hydrogel and the enantioselectivity was evaluated. The present work examined the effect of various factors such as running buffer pH and concentration or organic modifier on the chromatographic performances as well as binding characteristics of BSA for D,L-tryptophan (Trp). The retention and enantioseparation dramatically changed depending on the buffer pH and concentrations. These factors influenced EOF and especially binding characteristics of BSA for L-Trp. Under the optimized conditions, the BSA-encapsulated columns revealed the adequate repeatability concerning column-to-column and run-to-run.
Kato
Masaru
M
Department of Analytical Chemistry, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada Shizuoka, Shizuoka 422-8526, Japan.
Matsumoto
Nozomi
N
Sakai-Kato
Kumiko
K
Toyo'oka
Toshimasa
T
D000818:Animals; D002417:Cattle; D004339:Drug Compounding; D019075:Electrophoresis, Capillary / Q000379:methods; D005782:Gels; D011485:Protein Binding / Q000502:physiology; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013678:Technology, Pharmaceutical / Q000379:methods*
D005782:Gels; D012710:Serum Albumin, Bovine