THEORETICAL AND EXPERIMENTAL ASPECTS OF ENZYME DETERMINATION IN A CYTOCHEMICAL MODEL SYSTEM OF POLYACRYLAMIDE FILMS CONTAINING ALKALINE PHOSPHATASE | Zendy

P. van Duijn | Zendy; E. Pascoe | Zendy; M. van der Ploeg | Zendy

Open Access

THEORETICAL AND EXPERIMENTAL ASPECTS OF ENZYME DETERMINATION IN A CYTOCHEMICAL MODEL SYSTEM OF POLYACRYLAMIDE FILMS CONTAINING ALKALINE PHOSPHATASE

Author(s) -

P. van Duijn,

E. Pascoe,

M. van der Ploeg

Publication year - 1967

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 - 10.1177/15.11.631

Subject(s) - polyacrylamide , substrate (aquarium) , alkaline phosphatase , diffusion , chemistry , staining , enzyme , kinetics , biophysics , chromatography , analytical chemistry (journal) , biochemistry , polymer chemistry , biology , thermodynamics , ecology , physics , genetics , quantum mechanics

A theoretical treatment of the influence of slow substrate diffusion on the kinetics of an enzyme reaction in a cytochemical system is given. Quantitative aspects of the effect of several parameters on the diffusion of substrate were studied experimentally on a model consisting of polyacrylamide films into which alkaline phosphatase was incorporated. Spectra and staining intensity of the films were measured in a special film colorimeter. Enzyme activity in the films was determined cytochemically (with the azo dye coupling method) and biochemically. An effectiveness factor for which diffusion is not rate-limiting proved to be attainable with both methods.

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