Analysis of protein denaturation, aggregation and post-translational modification by agarose native gel electrophoresis.
Animals
Cattle
Dependovirus
/ genetics
Electrophoresis, Polyacrylamide Gel
/ methods
Glycated Hemoglobin
/ genetics
Humans
Hydrogen Peroxide
/ pharmacology
Phosphorylation
Protein Aggregates
Protein Denaturation
Protein Processing, Post-Translational
Proteolysis
Serum Albumin, Bovine
/ genetics
Sodium Dodecyl Sulfate
/ chemistry
Transferrin
/ genetics
Viral Proteins
/ genetics
ZAP-70 Protein-Tyrosine Kinase
/ genetics
Agarose
Antibody
BSA
Hemoglobin
Native gel
Transferrin
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 Mar 2021
01 Mar 2021
Historique:
received:
26
11
2020
revised:
09
01
2021
accepted:
12
01
2021
pubmed:
18
1
2021
medline:
30
4
2021
entrez:
17
1
2021
Statut:
ppublish
Résumé
Agarose native gel electrophoresis has been developed to separate proteins and protein complexes in the native state. Here, we applied this technology to analyze proteins that undergo degradation, post-translational modification or chemical/physical changes. Antibodies showed aggregation/association upon acid or heat treatment. Limited reduction of disulfide bonds resulted in non-covalent aggregation of bovine serum albumin and cleavage of only inter-chain linkages of an antibody that had no effects on its overall structure. Native agarose gel analysis showed changes in mobility of human transferrin upon Fe
Identifiants
pubmed: 33454336
pii: S0141-8130(21)00105-7
doi: 10.1016/j.ijbiomac.2021.01.075
pii:
doi:
Substances chimiques
Glycated Hemoglobin A
0
Protein Aggregates
0
Transferrin
0
Viral Proteins
0
hemoglobin A1c protein, human
0
Serum Albumin, Bovine
27432CM55Q
Sodium Dodecyl Sulfate
368GB5141J
Hydrogen Peroxide
BBX060AN9V
ZAP-70 Protein-Tyrosine Kinase
EC 2.7.10.2
ZAP70 protein, human
EC 2.7.10.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
589-596Informations de copyright
Copyright © 2021 Elsevier B.V. All rights reserved.