Localization of thiamine pyrophosphatase activity in motor end plates. | Zendy

István László | Zendy; T Bodor | Zendy

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Localization of thiamine pyrophosphatase activity in motor end plates.

Author(s) -

István László,

T Bodor

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 - 10.1177/29.5.6166663

Subject(s) - mediator , synaptic vesicle , neuromuscular junction , thiamine pyrophosphate , chemistry , thiamine , microbiology and biotechnology , ligation , free nerve ending , pyrophosphatase , neuroscience , biochemistry , biology , enzyme , anatomy , vesicle , membrane , cofactor

Thiamine pyrophosphatase (TPPase) activity was localized in the terminal arborization of the motor end plates both in rat and frog striated muscles. Electron microscopically the end product of the enzyme was seen in synaptic vesicles. That TPPase was axonally transported was indicated by its localization following experimental ligation of peripheral nerves. It is thus possible that TPPase may play a role in the synthesis of the synaptic mediator substance of the neuromuscular junction.

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