Native and Regenerated Bovine Albumin

Abstract

Investigation of the effect of denaturation on certain chemical, physicochemical, and biological properties of proteins has proved a valuable approach in the study of protein structure. Further advances have been made by a study of the reversal of the process of denaturation and by comparative measurements of the properties of a protein in the native and regenerated 1 states. Recently, evidence has been given to show that the denaturation of horse serum albumin (2) and of pseudoglobulin (3) by urea and guanldine hydrochloride are essentially irreversible processe s (4-6) although the regenerated proteins simulate certain characteristic properties of the native materials from which they were derived.

The Chemistry of Protein Denaturation.

“…Later work, on a crystalline fraction of horse serum albumin (295), indicated the molecular weight of the protein, denatured by 8 M urea or 8 M guanidine hydrochloride, to be essentially the same as that of the native form. This has been found to hold also for bovine serum albumin (331).…”

“…Thus, the axial ratio, calculated for a prolate ellipsoid of revolution and assuming 33 per cent hydration, was 3.3 for the native protein and 13.3 and 16.7 for serum albumin denatured by urea and by guanidine hydrochloride, respectively. Differences in the degree of denaturation were found between horse and beef serum albumin (331), and even between preparations of the latter when carried to different stages in the purification process. The effects of heattreatment on the molecular shape of serum albumin are small as compared with those produced by urea, and conceivably may be accounted for by an end-to-end aggregation of molecules of unchanged shape (118).…”

A Study of the Distribution of 2,4-Dinitrobenzene Sensitizers Between Isolated Lymph Node Cells and Extracellular Medium in Relation to Induction of Contact Skin Sensitivity

“…Rabbit serum aibnmln was prepared by ammonium sulfate precipitation (21). The molecular weights of these proteins were assumed to be 40,000 for ovalbumin, 70,000 for the serum albumins, and 160,000 for "y-globulin.…”

Gross and true ileal digestible amino acid contents of several animal body proteins and their hydrolysates

“…Further fractionation was carried out by precipitation of the plasma using ammonium sulphate (Putnam, Erickson, Volkin, & Neurath, 1943). The precipitated globulins fraction was separated from the albumin-enriched liquor by centrifugation.…”