Human serum albumin (HSA) is used in large amounts as an excipient in many biopharmaceutical formulation to prevent loss of the active ingredient through adsorption and/or degradation. Traditionally, iso-electric focusing has been used to demonstrate charge heterogeneity in HSA preparations. In an e
The standardization of the thiobarbituric acid assay for nonenzymatic glucosylation of human serum albumin
β Scribed by Kathryn A. Ney; Karen J. Colley; Salvatore V. Pizzo
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 494 KB
- Volume
- 118
- Category
- Article
- ISSN
- 0003-2697
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Proton relaxation enhancement (PRE) values for fatty acid spin labels bound to human serum albumin have been investigated using the inversion-recovery method at 24 MHz. At 0.1 mM protein concentration and a label-to-protein ratio of one-to-one, the PRE value for 12-Doxylsterate-albumin complex is 7.
The Cu-PTSM (pyruvaldehyde bis(N 4 -methylthiosemicarbazonato)copper-(II)) and Cu-ATSM (diacetyl bis(N 4 -methylthiosemicarbazonato)copper(II)) radiopharmaceuticals exhibit strong, species-dependent binding to human serum albumin (HSA), while Cu-ETS (ethylglyoxal bis(thiosemicarbazonato)copper(II))