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Arch Intern Med. 2002;162:356-358.

	Since this article does not have an abstract, we have provided the first 150 words of the full text and any section headings.

In 1984 we first reported that human serum albumin (HSA) in its denatured form was present in a large amount, up to 25% in terms of fully denaturated protein, in the serum of patients with chronic renal failure (CRF) and patients with the nephrotic syndrome (NS).¹ These results were obtained by studying urea levels in hydrolysates (supernatants) of HSA sampled from patients with CRF or NS.¹ A comparison of our findings with the literature led to a concept that changed our understanding of the pathophysiologic mechanisms and the nature of glomerulonephritis (GN).

Interaction Between Urea and Modified Serum Albumin

Serum HSA was found to interact easily with urea, a relatively inert substance generally regarded as merely the end product of metabolism, or a harmful substance in large concentrations. Urea is a weak cation. Its interaction with albumin is mainly of a noncovalent nature. In healthy individuals, one molecule of urea binds to the terminal COOH radical of . . . [Full Text of this Article]

Intrinsic Fluorescence of Chemically Purified Albumin

Probe Fluorescence Study of Conformational Properties of HSA

Clinical Findings

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