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Regulation of the interstitial distribution of plasma proteins

  • Chapter
Pathophysiology of Plasma Protein Metabolism

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Abstract

Albumin is a single polypeptide chain with over 580 amino acid residues—the complete sequence of which has recently been published1. The molecule has a covalent structure, the peptide chain being pictured as a series of double loops formed by disulphide bonds between 34 of its 35 half-cystine residues. This loop-and-link structure accounts for the well-known flexibility and stability of the molecule and contributes to its 20 day half-life in the body. Brown has drawn attention to the repeating triplet pattern in the loop arrangement and suggested that albumin can be considered as three domains. There is some homology in the amino acid sequence in each of the three domains, which leads to the suggestion that albumin originated from a molecule one-third of its present size. There are features in which albumin resembles the myoglobin molecule, but of immediate interest is the report that a 59 residue of human α-fetoprotein bears a striking homology to loops 2a and 2b of human albumin2, which suggests that this α1-globulin—produced in fetal life before albumin synthesis begins and by adult hepatocellular carcinomas—may be related genetically to albumin. There is no evidence that abnormal albumins are produced in liver diseases.

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Authors
  1. Victor M. Rosenoer
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  2. E. B. Reeve
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Editor information

Editors and Affiliations

  1. CNR Institute of Clinical Physiology, University of Pisa, Pisa, Italy

    Giuliano Mariani

  2. Fifth Medical Pathology, University of Pisa, Pisa, Italy

    Giuliano Mariani

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Rosenoer, V.M., Reeve, E.B. (1984). Regulation of the interstitial distribution of plasma proteins. In: Mariani, G. (eds) Pathophysiology of Plasma Protein Metabolism. Palgrave, London. https://doi.org/10.1007/978-1-349-06680-3_5

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