Ultrastructural localization of acetylcholinesterase in cultured cells. II. Cycloheximide-treated embryo muscle.
Author(s) -
T. K. Golder,
Pamela S. Nieberg,
BW Wilson
Publication year - 1977
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 - 10.1177/25.5.68070
Subject(s) - cycloheximide , acetylcholinesterase , embryo , aché , ultrastructure , intracellular , microbiology and biotechnology , biology , myocyte , enzyme , chemistry , protein biosynthesis , biochemistry , anatomy
The acetylcholinesterase activity (AChE) of cultured chick embryo muscle fibers that remains after the cells have been treated with the protein synthesis inhibitor cycloheximide was examined with cytochemical stains and the electron microscope. AChE activity that decreased rapidly after addition of the inhibitor was associated with enzyme within the cells, and AChE activity that was relatively insensitive to the inhibitor was associated with AChE outside of the cells. The results support the view that there are at least two fractions of AChE in developing muscle fibers, one intracellular and labile, the other extracelullar and stable.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom