A histochemical model dealing with an immobilized glucose oxidase-peroxidase system. The influence of diffusion limitations on histochemical results. | Zendy

Y. Malpièce | Zendy; Maithili Sharan | Zendy; J.N. Barbotin | Zendy; P Personne | Zendy; Thomas Deffieux | Zendy

Open Access

A histochemical model dealing with an immobilized glucose oxidase-peroxidase system. The influence of diffusion limitations on histochemical results.

Author(s) -

Y. Malpièce,

Maithili Sharan,

J.N. Barbotin,

P Personne,

Thomas Deffieux

Publication year - 1980

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.971

H-Index - 124

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/28.9.7410817

Subject(s) - horseradish peroxidase , peroxidase , glucose oxidase , chemistry , diffusion , substrate (aquarium) , immobilized enzyme , enzyme , membrane , oxidase test , biochemistry , chromatography , biophysics , biology , thermodynamics , ecology , physics

A histochemical model dealing with an immobilized bienzyme system (glucose oxidase-peroxidase) is presented. The model is an artificial proteic membrane obtained by a previously described co-cross-linking process. The kinetic properties of free and immobilized horseradish peroxidase were studied when 3,3'-diaminobenzidine is used as a hydrogen donor substrate. A new direct method was developed for immobilized enzyme activity measurements. Computer simulation based on experimental kinetic parameters was performed in order to discuss electron microscopy results. By changing diffusion limitations, various profiles of insoluble product were visualized inside the proteic film and no geometrical similarity was seen between enzyme distributions and insoluble osmiophilic product patterns.

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