Properties of acetylcholinesterase and non-specific cholinesterase in rat superior cervical ganglion and plasma.

Abstract:

:Amphiphile dependency, solubility in aqueous solutions, and sensitivity to proteolysis of acetylcholinesterase (AChE) and nonspecific cholinesterase (nsChE) in the rat superior cervical ganglion were studied and compared to properties of soluble plasma cholinesterases. Ganglion AChE shows strong amphiphile dependency: an amphyphilic substance must be present in the homogenizing medium in order to obtain maximal apparent enzyme activity. Apparent activity of AChE solubilized in Ringer's solution was also increased after subsequent addition of a detergent. The 4 S molecular form, predominant in this extract (corresponding to the fastest electrophoretic band), is very sensitive to papain proteolysis but can be protected by a detergent. This molecular form therefore carries an important hydrophobic domain and is probably membrane bound in situ. The 10 S form of ganglionic AChE, extracted in Ringer's solution, is probably a soluble enzyme since, like soluble plasma enzymes, it is not amphiphile dependent and is rather resistant to proteolysis. Ganglion nsChE is more water soluble, less amphiphile dependent and more protease resistant than AChE.

journal_name

Neurochem Res

journal_title

Neurochemical research

authors

Klinar B,Kamarić L,Sketelj J,Brzin M

doi

10.1007/BF00964537

subject

Has Abstract

pub_date

1985-06-01 00:00:00

pages

797-808

issue

6

eissn

0364-3190

issn

1573-6903

journal_volume

10

pub_type

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