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Clinical Chemistry 53: 2216, 2007; 10.1373/clinchem.2007.097071
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(Clinical Chemistry. 2007;53:2216.)
© 2007 American Association for Clinical Chemistry, Inc.

Letters to the Editor

A Receptor-Mediated Mechanism to Support Clinical Observation of Altered Albumin Variants

Jan Terje Andersen and Inger Sandlie

Department of Molecular, Biosciences, University of Oslo, Oslo, Norway

Address correspondence to the authors at: Department of Molecular Biosciences, University of Oslo, P.O. Box 1041, 0316 Oslo, Norway. Fax 47 22 85 40 61; e-mail janta@imbv.uio.no or inger.sandlie@imbv.uio.no.

The first 20% of the full text of this article appears below.


To the Editor:

Dolcini et al.(1) recently reported in this journal a novel splice-site mutation (denoted Bartin) that causes deletion of exon 11 in the human serum albumin (HSA) gene, ALB. In spite of their uncertain relevance to pathophysiology of diseases, differences in HSA sequence have interesting correlations with functional properties and stability. Bisalbuminemia (or alloalbuminemia) is a rare inherited or acquired condition characterized by the occurrence of 2 circulating components that are observed, typically, during routine clinical electrophoresis or in genetic surveys.

Over the past decades several cases of genetic polymorphisms, described in peer-reviewed papers and listed in the analbuminemia register(2), have been characterized as representing site-specific mutations, splice-site mutations, or frame-shift mutations. The deletion reported by Dolcini et al.(1) would give rise to a C-terminally truncated HSA variant of 410 . . . [Full Text of this Article]






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