Structural transition of bovine plasma albumin in the alkaline region the N‐B transition
- 12 January 1990
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 35 (1) , 1-11
- https://doi.org/10.1111/j.1399-3011.1990.tb00714.x
Abstract
Bovine plasma albumin (BPA) has approximately one SH group (Cys-34) which catalyzes the intramolecular SH, S-S exchange reaction in the alkaline region at low ionic strength, resulting in the formation of the aged form. So, the N-B transition at ionic strength above 0.20 and below 0.10 was studied using BPA and iodoacetamide-blocked BPA (IA-BPA), respectively. (1) pH profiles of [θ]262 and [θ]268 of BPA in 0.20m KCl showed the characteristic changes in the pH region 7.0-9.0, corresponding to the N-B transition. On going from pH 7.0 to 9.0 in 0.10 M KCl or NaCl, IA-BPA did not show significant changes in rotational relaxation times of tryptophyl fluorophors, CD-resolved secondary structures, spin-echo 1H-n.m.r. spectra and cross-relaxation times (T1S) between irradiated and observed protein protons, which might reflect the rigidity of the domains and/or subdomains. On the other hand, rotational relaxation times of l-anilino-8-naphthalenesulfonate-IA-BPA complex (IA-BPA-ANS0 9, molar ratio of ANS to IA-BPA = 0.9/1) showed significant decreases from 131 to 114ns on going from the N- to the B-forms in 0.10M KCl. The above results and reported experimental evidence might indicate that on going from the N- to the B-forms in 0.10 m KC1 or NaCl, the mutual movement of subdomains, connected with a flexible hinge region (Brown & Shockley (1982)) might increase without loss in the helicity and the rigidity of subdomains. (2) The N-B transition of IA-BPA in the absence of salt was quite different from those in 0.10 M KCl or NaCl. Decreases in the helicity and the intramolecular rigidity, as monitored by TIS-measurements, were observed on going from the N- to the B-forms.Keywords
This publication has 69 references indexed in Scilit:
- Sodium dodecyl sulfate-bovine plasma albumin complexInternational Journal of Peptide and Protein Research, 2009
- A proton nuclear magnetic resonance study of human serum albumin in the neutral pH regionBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Circular dichroic and fluorometric studies on the acid‐induced isomerization of bovine plasma albumin – 1‐anilino‐8‐naphthalenesulfonate complexInternational Journal of Peptide and Protein Research, 1985
- CD‐resolved secondary structure of bovine plasma albumin in acid‐induced isomerization*International Journal of Peptide and Protein Research, 1983
- The Rotational Diffusion of Albumin in Solutions of Connective‐Tissue PolysaccharidesEuropean Journal of Biochemistry, 1973
- Solvent Deuterium Isotope Effects on Acid-Base EquilibriaJournal of the American Chemical Society, 1964
- An Investigation of Bovine Plasma Albumin by Differential Ultraviolet Spectroscopy1Journal of the American Chemical Society, 1959
- The Availability of the Disulfide Bonds of Human and Bovine Serum Albumin and of Bovine γ-Globulin to Reduction by Thioglycolic AcidJournal of the American Chemical Society, 1957
- Structural Effects of the Interaction of Human Serum Albumin with Sodium Decyl Sulfate1Journal of the American Chemical Society, 1957
- Heterogeneity of the Binding Sites of Bovine Serum Albumin1Journal of the American Chemical Society, 1950