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THE HISTOCHEMICAL SPECIFICITY OF CHOLINESTERASES
Author(s) -
Richard D. Chessick
Publication year - 1954
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 - 10.1177/2.4.258
Subject(s) - cholinesterase , enzyme , substrate specificity , biochemistry , choline , chemistry , substrate (aquarium) , acetylcholinesterase , biology , ecology , pharmacology
On the basis of a review of the biochemical and histochemical literature, all esterases are divided into the eserine-resistant esterases (aliesterases) and the eserine-sensitive esterases (cholinesterases). It has previously been demonstrated by histochemical study that a wide spectrum of enzymes exists among the aliesterases; the present study is concentrated on the cholinesterases. The myoneural junction in four species; man, dog, rat, and mouse, was studied by histochemical techniques utilizing both choline esters and non-choline esters as substrates, and under the influence of various physical and chemical agents. On the basis of this study, it is demonstrated that none of the biochemical classifications or `types' of cholinesterases can be defended, and that the cholinesterases of the various species and tissues should therefore be viewed as a family of enzymes, forming a spectrum with multiple overlapping and differences with respect to physical properties, effects of inhibitors and substrate specificities.

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