Interaction between glycated serum albumin and AGE-receptors depends on structural changes and the glycation reagent

2012 ◽  
Vol 528 (2) ◽  
pp. 185-196 ◽  
Author(s):  
Venkata S.K. Indurthi ◽  
Estelle Leclerc ◽  
Stefan W. Vetter
Keyword(s):  
Serum Albumin ◽  
Structural Changes ◽  
Age Receptors

Influence of metal ions on thermal aggregation of bovine serum albumin: Aggregation kinetics and structural changes

2009 ◽  
Vol 103 (12) ◽  
pp. 1729-1738 ◽  
Author(s):  
Giovanna Navarra ◽  
Anna Tinti ◽  
Maurizio Leone ◽  
Valeria Militello ◽  
Armida Torreggiani
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Bovine Serum ◽  
Structural Changes ◽  
Aggregation Kinetics ◽  
Thermal Aggregation

Rapid detection and initial characterization of genetic variants of human serum albumin

1991 ◽  
Vol 37 (7) ◽  
pp. 1221-1224 ◽  
Author(s):  
J Merle Sheat ◽  
Robert J Peach ◽  
Peter M George
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Genetic Variants ◽  
Gel Electrophoresis ◽  
Structural Changes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl

Abstract We have studied the detection and classification of genetic variants of human serum albumin by electrophoresis. Samples from 10 patients who were heterozygous for eight different albumin variants were studied by two methods. In agarose gel electrophoresis, each of these variants has an abnormal mobility and can be classified on the basis that structural changes at the N-terminus abolish 63Ni binding. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis of whole serum, glycosylated variants are easily detected because of their greater apparent molecular mass.

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