Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

Scandium and Albumin

Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_200023

Definition

This contribution refers to the features of albumin and its interactions with scandium. Albumin is commonly found in blood plasma, and is unique to other plasma proteins in that it is not glycosylated. Albumin is the most abundant plasma protein in mammals and is produced in the liver and forms a large proportion of all plasma proteins. The human version is human serum albumin, and it normally constitutes about 60% of human plasma proteins. Human serum albumin is a single peptide chain of 585 amino acids, held in three homologous domains by 17 disulfide bonds. Within each domain are two long loops plus one shorter loop. The S–S bonds provide stability while the intervening peptide strands allow for flexibility. The configuration includes 67% alpha helix and 10% beta turn.

The main function of albumin is to regulate the colloidal osmotic pressure needed for proper distribution of body fluids between intravascular compartments and body tissues. It also binds water, cations...

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References

  1. Bal W, Christodoulou J, Sadler P, Tucker A (1998) Multi-metal binding site of serum albumin. J Inorg Biochem 70:33–39CrossRefPubMedGoogle Scholar
  2. Banerjee A, Lahiri S (2009) Albumin metal interaction: a multielemental radiotracer study. J Radioanal Nucl Chem 279:733–741CrossRefGoogle Scholar
  3. Rosoff B, Spencer H (1979) Binding of rare earths to serum proteins and DNA. Clin Chim Acta 93:311–319CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety & CAS Key Laboratory of Nuclear Analytical TechniquesInstitute of High Energy Physics, Chinese Academy of SciencesBeijingChina