STARCH GEL ELECTROPHORESIS OF BRAIN ESTERASES | Zendy

Kevin D. Barron | Zendy; Joseph Bernsohn | Zendy; A R HESS | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

STARCH GEL ELECTROPHORESIS OF BRAIN ESTERASES

Author(s) -

Kevin D. Barron,

Joseph Bernsohn,

A R HESS

Publication year - 1961

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 - 10.1177/9.6.656

Subject(s) - acetylthiocholine , acetylcholinesterase , chemistry , enzyme , biochemistry , cholinesterase , chromatography , iodide , substrate (aquarium) , hydrolysis , starch , electrophoresis , gel electrophoresis , aché , organic chemistry , biology , endocrinology , ecology

1. Starch gel electrophoresis of rat brain homogenates has demonstrated 9 esterases which hydrolyze α-naphthyl acetate and naphthol AS-acetate. One of these has been identified as acetylcholinesterase. The nature of the others is undefined. In addition an enzyme (presumably pseudocholinesterase) acting against butyrylthiocholine iodide has been located at the site of sample insertion. 2. Homogenates of human white matter have yielded 9 esterases active against the same naphthol substrates. None of these is a cholinesterase. However, with acetylthiocholine iodide as substrate, acetylcholinesterase is demonstrable in human material. Enzymic activity against butyrylthiocholine iodide is demonstrable at the origin in human material, also. 3. Best results are obtained by use of homogenates centrifuged at 20,000 x g for 60 minutes.

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