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: The binding of cupric ions to 1-carboxymethylhistidine-119-ribonuclease.
    Author: Saundry RH, Stein WD.
    Journal: Biochem J; 1968 Jul; 108(4):583-6. PubMed ID: 5667270.
    Abstract:
    Binding of Cu(2+) by 1-carboxymethylhistidine-119-ribonuclease was investigated by using diligand metal ion buffers. A single Cu(2+)-binding site was found over the Cu(2+) concentration range studied. The binding constants for this site were 8.33x10(5) (+/-2%)m(-1) and 1.57x10(4) (+/-6%)m(-1) at pH7.0 and 6.1 respectively. An estimate of the pH-independent Cu(2+)-binding constant suggests that the most avid Cu(2+)-binding site has disappeared after carboxymethylation. This is consistent with an earlier report that binding of Cu(2+) at the most avid site is associated with the loss of enzymic activity.
    [Abstract] [Full Text] [Related] [New Search]