Literature DB >> 24233881

Protection of immobilized sulfhydryl groups against autooxidation by alterations in their microenvironment.

A M Klibanov1, T E Barta.   

Abstract

Immobilized sulfhydryl groups were prepared by partial thiolation of NH2-glass beads. The microenvironment of the immobilized SH groups was varied by different chemical modifications of neighboring NH2 groups. Introduction of a strong charge in the surroundings of immobilized sulfhydryls results in their dramatic stabilization against autooxidation. This effect is due to the salting of O2 from the surface microlayer of the thiolated beads.

Entities:  

Year:  1981        PMID: 24233881     DOI: 10.1007/BF02780798

Source DB:  PubMed          Journal:  Appl Biochem Biotechnol        ISSN: 0273-2289            Impact factor:   2.926


  7 in total

1.  Tissue sulfhydryl groups.

Authors:  G L ELLMAN
Journal:  Arch Biochem Biophys       Date:  1959-05       Impact factor: 4.013

2.  The sulfur chemistry of proteins.

Authors:  R CECIL; J R McPHEE
Journal:  Adv Protein Chem       Date:  1959

3.  Thiol groups of biological importance.

Authors:  E S G BARRON
Journal:  Adv Enzymol Relat Subj Biochem       Date:  1951

4.  Quantitative determination of amino groups on derivatized controlled pore glass: a comparison of methods.

Authors:  C C Lee; G M Loudon
Journal:  Anal Biochem       Date:  1979-04-01       Impact factor: 3.365

5.  Porous glass for affinity chromatography applications.

Authors:  H H Weetall; A M Filbert
Journal:  Methods Enzymol       Date:  1974       Impact factor: 1.600

6.  Preparation of the bifunctional enzyme ribonuclease-deoxyribonuclease by cross-linkage.

Authors:  D Wang
Journal:  Biochemistry       Date:  1979-10-02       Impact factor: 3.162

7.  A rationale for stabilization of oxygen-labile enzymes: application to a clostridial hydrogenase.

Authors:  A M Klibanov; N O Kaplan; M D Kamen
Journal:  Proc Natl Acad Sci U S A       Date:  1978-08       Impact factor: 11.205

  7 in total

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