Effective charge of bovine serum albumin determined by ...
Feb 19, 2007 · The effective charge of bovine serum albumin in aqueous solution is determined by dynamic NMR as a function of pH. The effective charge results from the degree of dissociation varying with pH and the local counterion condensation.
Bovine serum albumin - Wikipedia
Bovine serum albumin (BSA or "Fraction V") is a serum albumin protein derived from cows. It is often used as a protein concentration standard in lab experiments.
Electrostatic Unfolding and Interactions of Albumin Driven by ...
During the N–F isoform transition, bovine serum albumin (BSA) passes through its isoelectric point at pH 4.7 and the net charge on the protein changes from −16 at pH 7.4 to +100 at pH 3.5. 9 Low solution pH also shifts the denaturation temperature of BSA from 62 °C (at pH 7.4) to 46.8 °C (at pH 3.5). 38 In concentrated solutions, we have ...
Specific charge of the BSA molecules at different pH values
Bovine serum albumin (BSA) that was acidified and hydrolysed with pepsin, showed the highest extent and most efficient hydrolysis by trypsin.
Electrical characterization of protein molecules by a solid ...
Jul 7, 2007 · The authors measured the change in protein charge of bovine serum albumin (BSA) protein induced by pH variation. They also confirmed that BSA molecules indeed traverse nanopores using an improved chemiluminescent analysis.
On the aggregation of bovine serum albumin - ScienceDirect
Mar 1, 2022 · The present work shows that the aggregation behaviour of bovine serum albumin in solution and its modulation by salt ions can be explained by chemical concepts, with chemical equilibrium playing an essential role.
Effective charge of bovine serum albumin determined by ...
Feb 19, 2007 · This work reports a study on bovine serum albumin cold-gelation induced by copper or zinc ions, and shows that the elastic behaviour depends on ion concentration and gels obtained in the presence of zinc exhibit an elastic value larger than …