Literature DB >> 172068

A method for investigating the effect of temperature on the 695 nm band of insoluble cytochrome c.

T A Moore, C Greenwood.   

Abstract

A method is described for computer analysis of simple spectrophotometric changes in particulate systems, and this has been applied to the bleaching of the 695 nm band of insoluble ferricytochrome c by temperature. The results show that insolubilization has no effect on the standard enthalpy change but lowers the value for the standard entropy change. This effect appears to be independent of the concentration of the gel matrix to which the cytochrome c is bound, but dependent on the ionic strength of the surrounding solution.

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Year:  1975        PMID： 172068      PMCID： PMC1165603          DOI： 10.1042/bj1490169

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  15 in total

1.  THE 695-MMM. BAND OF FERRICYTOCHROME C AND ITS RELATIONSHIP TO PROTEIN CONFORMATION.

Authors:  A SCHEJTER; P GEORGE
Journal:  Biochemistry       Date:  1964-08       Impact factor: 3.162

2.  HORSE HEART CYTOCHROME C. SPECTROPHOTOMETRIC TITRATION AND VISCOSITY CHANGES IN ALKALINE SOLUTION.

Authors:  J A RUPLEY
Journal:  Biochemistry       Date:  1964-11       Impact factor: 3.162

3.  Spectrum of horse-heart cytochrome c.

Authors:  E MARGOLIASH; N FROHWIRT
Journal:  Biochem J       Date:  1959-03       Impact factor: 3.857

4.  Some changes in the reactivity of enzymes resulting from their chemical attachment to water-insoluble derivatives of cellulose.

Authors:  W E Hornby; M D Lilly
Journal:  Biochem J       Date:  1968-05       Impact factor: 3.857

5.  Studies on ferricytochrome c. I. Effect of pH, ionic strength and protein denaturants on the spectra of ferricytochrome c.

Authors:  C Greenwood; M T Wilson
Journal:  Eur J Biochem       Date:  1971-09-13

6.  Studies on pH-activity profiles of an immobilized two-enzyme system.

Authors:  S Gestrelius; B Mattiasson; K Mosbach
Journal:  Biochim Biophys Acta       Date:  1972-08-28

7.  Changes in conformation of insolubilized trypsin and chymotrypsin, followed by fluorescence.

Authors:  D Gabel; I Z Steinberg; E Katchalski
Journal:  Biochemistry       Date:  1971-12-07       Impact factor: 3.162

8.  The chemical attachment of chymotrypsin to water-insoluble polymers using 2-amino-4,6-dichloro-s-triazine.

Authors:  G Kay; M D Lilly
Journal:  Biochim Biophys Acta       Date:  1970-02-11

Review 9.  Water-insoluble derivatives of enzymes, antigens, and antibodies.

Authors:  I Silman; E Katchalski
Journal:  Annu Rev Biochem       Date:  1966       Impact factor: 23.643

10.  The preparation and properties of ficin chemically attached to carboxymethylcellulose.

Authors:  W E Hornby; M D Lilly; E M Crook
Journal:  Biochem J       Date:  1966-02       Impact factor: 3.857
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  3 in total

1.  Properties of cytochrome c modified by attachment to a carbohydrate polymer.

Authors:  M C Silvestrini; A Colosimo; M Brunori; E Antonini
Journal:  Biochem J       Date:  1978-02-01       Impact factor: 3.857

2.  An investigation of protein conformation of cytochrome c by using cytochrome c insolubilized on to agarose gel.

Authors:  C Greenwood; T A Moore
Journal:  Biochem J       Date:  1976-02-01       Impact factor: 3.857

3.  An extremely thermostable xylanase from the thermophilic eubacterium Thermotoga.

Authors:  H D Simpson; U R Haufler; R M Daniel
Journal:  Biochem J       Date:  1991-07-15       Impact factor: 3.857
  3 in total

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