Circular dichroic and 1 H-NMR studies on the aged form of bovine plasma albumin
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1991.tb01437.x/fullpdf
Reference30 articles.
1. Microheterogeneity of plasma albumins. V. Permutations in disulfide pairings as a probable source of microheterogeneity in bovine albumin
2. Reversible sulfhydryl-catalyzed structural alteration of bovine mercaptalbumin
3. Sulfhydryl-catalyzed isomerization of bovine mercaptalbumin
4. SS-interchanged and oxidized isomers of bovine serum albumin separated by isoelectric focusing
5. Spontaneous in vivo isomerization of bovine serum albumin as a determinant of its normal catabolism.
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3. Analysis of local polarity change around Cys34 in bovine serum albumin during N→B transition by a polarity-sensitive fluorescence probe;Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy;2009-09
4. 1H-NMR and CD studies on the structural transition of serum albumin in the acidic region-The N→F transition;The Journal of Peptide Research;2009-01-12
5. Comparative 1H NMR studies on the structural looseness of the aged (A) and non-aged (N) bovine mercaptalbumin in the alkaline region;International Journal of Biological Macromolecules;2009-01
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