Literature DB >> 1430791

A new micromethod for mechano-chemical research.

V N Morozov1, A V Gorelov, T A Zenchenko.   

Abstract

A new micromethod to study activity of enzymes in crystalline and amorphous solid samples subjected to tension is described. Both static (up to 200%) and dynamic (with an amplitude up to 50% and frequency of 10(-3)-50 Hz) deformation may be applied to the sample during the activity measurement. Strain-induced changes in activity of thin (3-10 microns) needle-like strips (0.2-0.5 microns long), cut out of the microtome sections of cross-linked crystals of pancreatic carboxypeptidase A is measured in a droplet of substrate solution (with volume of 10(-6)-10(-9) l) with a pH-microelectrode technique.

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Year:  1992        PMID: 1430791     DOI: 10.1016/0165-022x(92)90035-9

Source DB:  PubMed          Journal:  J Biochem Biophys Methods        ISSN: 0165-022X


  1 in total

1.  Mechanical deformation enhances catalytic activity of crystalline carboxypeptidase A.

Authors:  T A Zenchenko; V N Morozov
Journal:  Protein Sci       Date:  1995-02       Impact factor: 6.725

  1 in total

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