The Denaturation of Albumin

Abstract

Man is incurably empirical. When a given experiment fails to produce the expected result, he says it will not work. Whereas, were he neither empirical nor dogmatic he would say that it does not work.When egg albumin or egg white, as the case may be, is heated to a certain temperature, coagulation of the suspended particles takes place. Because people, in the past, failed to repeptize the gel so formed, it has been tacitly assumed that it cannot be restored chemically unaltered, at least, to the original colloidal state. Some profound change has been held responsible for this failure of the albumin to repeptize. This apparent set of circumstances left an opportunity open to coin a word; the term "denaturation" or "denaturization" resulted inevitably.Much has been written about "denaturation", for instance, the following:* 1 * This work is part of the programme now being carried out at

Biomineralized Gd2O3@HSA Nanoparticles as a Versatile Platform for Dual‐Modal Imaging and Chemo‐Phototherapy‐Synergized Tumor Ablation

“…Plausible explanations are as follows. During the Synthesis process of Gd 2 O 3 @HSA NPs, the existence of heavy metal ion Gd 3+ and alkaline reaction environment (pH = 12) probably changed or destroyed the spatial structure of albumin as a result of local denaturation . This behavior might induce the enhancement of hydrophobicity and the formulation of intermolecular oligomerization of albumin, thereby resulting in slower drug release rate compared with PIH NPs.…”

Studies on the gluten proteins /

“…They were of the opinion that this lowering was due to the solubility effect of urea and were there no such effect, the addition of urea would increase the viscosity. Bancroft and Rutzler (6) reported that the extraction of aqueous solutions of egg whites with ether prevented the coagulation of egg albumin by alcohol and heat.…”