Literature DB >> 486497

4-Hydroxy-3-nitrophenylglyoxal. A chromophoric reagent for arginyl residues in proteins.

C L Borders, L J Pearson, A E McLaughlin, M E Gustafson, J Vasiloff, F Y An, D J Morgan.   

Abstract

The chromophoric reagent, 4-hydroxy-3-nitrophenylglyoxal, is highly selective for the modification of arginine in aqueous solution at pH 7--9. The reagent also inactivates creatine kinase (ATP:creatine N-phosphotransferase, EC 2.7.3.2) in a manner analogous to that reported with phenylglyoxal.

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Year:  1979        PMID: 486497     DOI: 10.1016/0005-2744(79)90319-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

Review 1.  Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.

Authors:  Xiaoran Roger Liu; Mengru Mira Zhang; Michael L Gross
Journal:  Chem Rev       Date:  2020-04-22       Impact factor: 60.622

2.  Studies on inactivation of anion transport in human red blood cell membrane by reversibly and irreversibly acting arginine-specific reagents.

Authors:  T Julien; L Zaki
Journal:  J Membr Biol       Date:  1988-06       Impact factor: 1.843

3.  Selective phenylglyoxalation of functionally essential arginyl residues in the erythrocyte anion transport protein.

Authors:  P J Bjerrum; J O Wieth; C L Borders
Journal:  J Gen Physiol       Date:  1983-04       Impact factor: 4.086

  3 in total

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