Different behavior of Ferguson plot between agarose and polyacrylamide gels.

Agarose gel Ferguson plot Native gel electrophoresis Polyacrylamide gel

Journal

Biophysical chemistry
ISSN: 1873-4200
Titre abrégé: Biophys Chem
Pays: Netherlands
ID NLM: 0403171

Informations de publication

Date de publication:
13 Feb 2024
Historique:
received: 14 11 2023
revised: 04 02 2024
accepted: 12 02 2024
medline: 18 2 2024
pubmed: 18 2 2024
entrez: 17 2 2024
Statut: aheadofprint

Résumé

In this study, we conducted Ferguson plot analyses using both agarose and polyacrylamide gels in native electrophoresis and SDS-PAGE. The results revealed intriguing differences in the behavior of bovine serum albumin (BSA) and other model proteins. Specifically, BSA exhibited Ferguson plot slopes that were dependent on the oligomer size in agarose native gel electrophoresis, while such size-dependent behavior was not observed in native-PAGE or SDS-PAGE. These findings suggest that Ferguson plot analysis is a suitable approach when using agarose gel under the electrophoretic conditions employed in this study. Furthermore, our investigation extended to model proteins with acidic isoelectric points and larger molecular weights, namely Ferritin and caseinolytic peptidase B (ClpB). Notably, these proteins displayed distinct Ferguson plot slopes when subjected to agarose gel electrophoresis. Intriguingly, when polyacrylamide gel was employed, ClpB exhibited multiple bands, each with its unique Ferguson plot slope, deviating from the expected behavior based on molecular size. This divergence in Ferguson plot characteristics between agarose and polyacrylamide gels points to an interesting and complex interplay between protein properties and gel electrophoresis conditions.

Identifiants

pubmed: 38367540
pii: S0301-4622(24)00029-2
doi: 10.1016/j.bpc.2024.107200
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

107200

Informations de copyright

Copyright © 2024 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest This work was supported by Kyokuto Pharmaceutical Industrial Co., Ltd. Y.T., and T.A. (Teruo Akuta) are employees of the for-profit company Kyokuto Pharmaceuticals. M.T. is emeritus professor of the Kagoshima university and has no conflict of interest. T.A. (Tsutomu Arakawa) used to belong to the for-profit company Alliance Protein Laboratories but currently has no conflict of interest.

Auteurs

Yui Tomioka (Y)

Product Development Division, Kyokuto Pharmaceutical Industrial Co., Ltd., 3333-26, Aza-Asayama, Kamitezuna Takahagi-shi, Ibaraki 318-0004, Japan. Electronic address: y.tomioka@kyokutoseiyaku.co.jp.

Teruo Akuta (T)

Product Development Division, Kyokuto Pharmaceutical Industrial Co., Ltd., 3333-26, Aza-Asayama, Kamitezuna Takahagi-shi, Ibaraki 318-0004, Japan. Electronic address: t.akuta@kyokutoseiyaku.co.jp.

Masao Tokunaga (M)

Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, Korimoto, Kagoshima-shi 890-0065, Japan.

Tsutomu Arakawa (T)

Alliance Protein Laboratories, 13380 Pantera Rd, San Diego, CA 92130, USA. Electronic address: tarakawa2@aol.com.

Classifications MeSH