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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
NATIVE AND REGENERATED BOVINE ALBUMIN : I. PREPARATION AND PHYSICOCHEMICAL PROPERTIES
F W Putnam1, J O Erickson, E Volkin
1Department of Biochemistry, Duke University, School of Medicine, Durham.
The Journal of General Physiology
|October 30, 2009
Summary
Researchers purified and characterized bovine albumin, finding it denatures easily but can be regenerated. Regenerated albumin shows near-native properties but retains some denaturation characteristics, impacting tryptic digestion.
Area of Science:
- Biochemistry
- Protein Chemistry
Background:
- Bovine albumin is a key protein with diverse applications.
- Understanding its structural properties and denaturation behavior is crucial for biochemical research.
Purpose of the Study:
- To prepare and characterize homogeneous bovine albumin.
- To investigate the denaturation and regeneration properties of bovine albumin.
Main Methods:
- Ammonium sulfate precipitation and isoelectric precipitation for protein purification.
- Physicochemical analyses including viscosity, diffusion, sedimentation, and electrophoresis.
- Denaturation studies using urea and guanidine hydrochloride, followed by regeneration experiments.
Main Results:
- Homogeneous bovine albumin was prepared with 0.38% carbohydrate and 15.2% nitrogen.
- Native albumin has a molecular weight of 65,000 and a prolate ellipsoid shape.
- Bovine albumin readily denatures in concentrated urea/guanidine hydrochloride but can be regenerated with 95% yield.
- Regenerated albumin closely resembles native albumin but shows altered tryptic digestion susceptibility.
Conclusions:
- Bovine albumin can be effectively purified and its properties characterized.
- Denaturation and regeneration studies reveal insights into protein folding and stability.
- While regeneration restores many properties, subtle differences persist, indicating a residual denatured state.
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