Literature DB >> 7380607

Chemical modification of methionines of ribonuclease A with o-benzoquinone.

M N Gupta, P J Vithayathil.   

Abstract

The accessibility of methionines in RNAase A to reaction with OBQ has been studied at highly acidic pH. The differences between the rate constants of reactions of the methionine and methionines of RNAase A with OBQ is a reflection on the limited accessibility of methionines in the protein conformation. Nevertheless, at sufficiently high OBQ concentration, all the four methionines of the enzyme can be modified. At lower concentration of OBQ, a derivative may be prepared in which a specific methionine is modified. The introduced chromophore ionizes at around pH 3 in this derivative. The derivative has partial activity towards RNA which is enhanced on addition of S-protein.

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Year:  1980        PMID: 7380607     DOI: 10.1111/j.1399-3011.1980.tb02572.x

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  1 in total

Review 1.  Chemical Reactivities of ortho-Quinones Produced in Living Organisms: Fate of Quinonoid Products Formed by Tyrosinase and Phenoloxidase Action on Phenols and Catechols.

Authors:  Shosuke Ito; Manickam Sugumaran; Kazumasa Wakamatsu
Journal:  Int J Mol Sci       Date:  2020-08-24       Impact factor: 5.923

  1 in total

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