Structural analysis and fatty acid-binding properties of two Croatian variants of human serum albumin |
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Authors: | Kragh-Hansen Ulrich Campagnoli Monica Dodig Slavica Nielsen Henning Benko Bojan Raos Miljenko Cesati Roberto Sala Alberto Galliano Monica Minchiotti Lorenzo |
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Institution: | Department of Medical Biochemistry, University of Aarhus, DK-8000 Aarhus C, Denmark. ukh@biokemi.au.dk |
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Abstract: | BACKGROUND: The aim of the present work was to characterize the molecular defects of a slow-migrating (albumin Zagreb) and a fast-migrating (albumin Krapina) genetic variant of human serum albumin detected in heterozygous persons living in Croatia and to elucidate the fatty acid-binding properties of the two alloalbumins. METHODS: Purification and structural identification of the variants were performed by conventional protein chemistry methods, whereas types and amounts of albumin-bound, endogenous fatty acids were determined by gas chromatography. RESULTS: Protein sequencing established that albumin Zagreb is a proalbumin variant (-1Arg-->Gln), and that albumin Krapina is due to a mutation within the mature polypeptide chain (573Lys-->Glu). The gas chromatographic results showed that the fatty acid-binding properties of the proalbumin variant are normal, while the amino acid substitution in position 573 resulted in a general decrease of fatty acid binding. CONCLUSIONS: The structural defects of the first alloalbumins, detected by routine clinical electrophoresis among the Croatian population, were characterized. Albumin Zagreb is caused by a hot-spot mutation occurring in a CpG sequence in the albumin gene. It is commonly assumed that bisalbuminaemia has no direct clinical relevance. However, the present study suggests that naturally occurring mutations can affect the ligand-binding properties of human serum albumin. |
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