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pro vyhledávání: '"Patricia Richier"'
Publikováno v:
European Journal of Biochemistry. 207:1101-1108
We analyzed the molecular forms of acetylcholinesterase (AChE) in the nematode Steinernema carpocapsae. Two major AChEs are involved in acetylcholine hydrolysis. The first class of AChE is highly sensitive to eserine (IC50 = 0.05 microM). The corresp
Publikováno v:
Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 1992, pp.83-88
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 1992, pp.83-88
The type of membrane association of acetylcholinesterase (AChE, EC 3.1.1.7) was studied in rabbit lymphocytes and erythrocytes. In both cases, the unique AChE molecular form was an amphiphilic dimer (referred to as G2a) anchored in the membrane by a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47d2e7f36cd3c55be94102ec42abc645
https://hal.inrae.fr/hal-02703660
https://hal.inrae.fr/hal-02703660
Autor:
Patricia Richier, Jean-Pierre Toutant, Martine Arpagaus, Danielle Thierry-Mieg, Yann L'hermite, Florence Le Roy, Jean Baptiste Berge
Publikováno v:
Multidisciplinary approaches to cholinesterase functions
Multidisciplinary approaches to cholinesterase functions, Plenum press, 1992
Multidisciplinary Approaches to Cholinesterase Functions ISBN: 9781461363286
Multidisciplinary approaches to cholinesterase functions, Plenum press, 1992
Multidisciplinary Approaches to Cholinesterase Functions ISBN: 9781461363286
In vertebrates, acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are polymorphic enzymes presenting both globular and asymmetric forms1. In invertebrates, only AChE has been characterized so far that presents a reduced molecular diversity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2733eea4b7a251275de5f6b093ce991
https://hal.inrae.fr/hal-02846700
https://hal.inrae.fr/hal-02846700