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

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Heat and cold denaturation of beta-lactoglobulin B.
    Author: Azuaga AI, Galisteo ML, Mayorga OL, Cortijo M, Mateo PL.
    Journal: FEBS Lett; 1992 Sep 14; 309(3):258-60. PubMed ID: 1516695.
    Abstract:
    The thermal denaturation of bovine beta-lactoglobulin B was investigated by high-sensitivity differential scanning microcalorimetry between pH 1.5 and 3.0 in 20 mM phosphate buffer. The process was found to be a reversible, two-state transition. Progressive addition of guanidine hydrochloride at pH 3.0 leads to the appearance of a low-temperature calorimetric endotherm, corresponding to the cold renaturation of the protein. Circular dichroism experiments have confirmed the low and high temperature denaturation processes, and have shown some structural differences between both denatured states of beta-lactoglobulin B.
    [Abstract] [Full Text] [Related] [New Search]