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http://dx.doi.org/10.1001/jama.203.3.180 | DOI Listing |
Clin Lab
April 2013
Centre of Clinical Laboratory, University Hospital "St. George" Plovdiv, Bulgaria.
Background: Bisalbuminemia or alloalbuminemia is a rare inherited or acquired condition characterized by the presence of two albumin fractions during electrophoretical separation of serum proteins.
Methods: Bisalbuminemia was incidentally detected by agarose gel electrophoresis (AGE) during standard laboratory investigation of a 36-year old female patient, referred to our laboratory with the diagnosis of immune thrombocytopenia.
Results: The electrophoregram showed dysproteinemia with the presence of two distinct albumin bands.
Clin Chim Acta
June 1999
Department of Pathology, University of Texas Southwestern Medical Center, Dallas 75235-9073, USA.
Bisalbuminemia (or alloalbuminemia) is a relatively rare hereditary or acquired condition characterized by the presence of two distinct albumin bands, or, less commonly, a single widened albumin band, after agarose gel electrophoresis of serum. Bisalbumins are caused by point- or chain-mutations that occur with a population frequency of 1:10,000 to 1:1000. Although no adverse clinical effects have been attributed to bisalbumins, some albumin variants have altered affinity for steroid hormones, thyroxine, or drugs.
View Article and Find Full Text PDFRyoikibetsu Shokogun Shirizu
March 1999
Department of Internal Medicine, Niigata Prefectural Central Hospital.
Ryoikibetsu Shokogun Shirizu
September 1998
Department of Biological Science and Technology, Faculty of Engineering, University of Tokushima.
Eur J Biochem
July 1997
Dipartimento di Biochimica A. Castellani, Università di Pavia, Italy.
A long-term electrophoretic survey on plasma proteins, which was carried out in several clinical laboratories in Italy, identified 28 different genetic variants of human serum albumin and four cases of analbuminemia. We have previously characterized 16 point mutations, 3 C-terminal mutants, and the genetic defects in two analbuminemic subjects. Here, we report the molecular defects of four alloalbumins that have been characterized by protein structural analysis.
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