These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Modified β-casein restores thermal reversibility of human carbonic anhydrase II: the salt bridge mechanism.
    Author: Fallah-Bagheri A, Moosavi-Movahedi AA, Taghizadeh M, Khodarahmi R, Ma'mani L, Bijari N, Bohlooli M, Shafiee A, Sheibani N, Saboury AA.
    Journal: Biotechnol Appl Biochem; 2013; 60(3):298-304. PubMed ID: 23621563.
    Abstract:
    Modified β-casein (mβ-CN) was investigated as an efficient additive for thermal reversibility of human carbonic anhydrase II (HCA II) at pH 7.75. The mβ-CN was obtained via modification of β-casein (β-CN) acidic residues using Woodward's reagent K. The effects of mβ-CN on the reversibility and stability of HCA II were determined by differential scanning calorimetry, UV-vis, and 1-anilinonaphthalene-8-sulfonic acid fluorescence spectroscopic methods. The mβ-CN, as an additive, enhanced thermal reversibility of HCA II by 33%. Together, our results indicated that mβ-CN is very efficient in decreasing thermal aggregation and enhancing the stability of HCA II. Using theoretical studies, we propose that the mechanism for thermal reversibility is mediated through formation of a salt bridge between the Woodward part of mβ-CN and the Zn ion of HCA II.
    [Abstract] [Full Text] [Related] [New Search]