Kinetic, computer, and electron microscopic studies dealing with an artificial enzyme membrane: theoretical and experimental evaluation of the cytochemical demonstration of acetylcholinesterase. | Zendy

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

Open Access

Kinetic, computer, and electron microscopic studies dealing with an artificial enzyme membrane: theoretical and experimental evaluation of the cytochemical demonstration of acetylcholinesterase.

Author(s) -

Y. Malpièce,

Maithili Sharan,

J.N. Barbotin,

P Personne,

Thomas Deffieux

Publication year - 1981

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 - 10.1177/29.5.7252129

Subject(s) - glutaraldehyde , acetylcholinesterase , bifunctional , chemistry , membrane , kinetic energy , biophysics , enzyme , chromatography , biochemistry , catalysis , biology , physics , classical mechanics

The cytochemical demonstration of acetylcholinesterase is theoretically and experimentally evaluated with a model system. The model is an artificial proteic membrane in which acetylcholinesterase homogeneously is immobilized chemically by a bifunctional agent, glutaraldehyde. The copper-thiocholine histochemical method is studied kinetically and the system is simulated by computer calculations based on experimental kinetic parameters and numerical analysis methods. In addition, the corresponding electron micrographs are presented. These studies lead to the conclusions that the system is ruled by diffusional constraints and that enzyme distribution and repartition of the insoluble electron dense product are not circumscribed by any specific conditions.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research