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Enzyme
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Target Concepts:
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Enzyme
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Query: EC:3.1.1.7 (
acetylcholinesterase
)
28,390
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Normal muscle spindles of human skeletal muscle were studied histochemically. 1) Four histochemical types of intrafusal muscle fibers were classified by ATPase stain: Bag I fiber, Bag II fiber, Chain I fiber and Chain II fiber. Moreover, two types of nuclear bag fibers were classified by
NADH
Tetrazolium Reductase stain and PAS stain: Bag I fiber and Bag II fiber. 2) Three kinds of fusimotor endings were verified by the
cholinesterase
technic: en plaque, en grappe and diffuse endings. 3) Two kinds of fusisensory endings were verified by
NADH
TR stain and also electron-microscopically: primary and secondary sensory endings.
...
PMID:Histochemical study of normal human muscle spindle. Histochemical classification of intrafusal muscle fibers and intrafusal nerve endings. 7 4
Normal and diseased human muscle cells have been grown in combined cultures with 12-14 day embryonic mouse spinal cord explants. Nerve endings on myotubes were found by light and scanning electron microscopy, and motor end-plates were identified by a histochemical reaction for
acetylcholinesterase
. Contracting myotubes, never observed in cultures of human muscle alone, were found in a culture from normal muscle. Histochemical studies demonstrated the presence of strongly and weakly reacting myotubes for both ATPase pH 9.4 and
NADH
-TR, but could not be related to the development of fibre types. No differences in morphology or histochemical reactions were found between normal and diseased muscle cells in these combined cultures.
...
PMID:Growth of diseased human muscle in combined cultures with normal mouse embryonic spinal cord. 12 4
Exposure of rat brain Na+ + K+-ATPase (ATP phosphohydrolase E.C. 3.6.1.3) to concentrations of cassaine greater than 1 x 10(-4) M resulted in a poorly reversible inhibition of this enzyme. Inhibition did not require the presence of ATP and developed rapidly, but the final amount of inhibition observed was independent of time. The amount of inhibition observed at a given concentration of cassaine was reduced by increasing the concentration of membranes in the system. The inhibition of Na+ + K+-ATPase activity was associated with equivalent inhibition of the phosphorylation and (3H)-ouabain binding reactions of this enzyme, while the uninhibited enzyme was apparently kinetically normal. Concentrations of cassaine which produced this stable inhibition of Na+ + K+-ATPase had no effect on the Mg2+-activated ATPase or the
NADH
cytochrome-c-reductase activities of crude rat brain microsomal preparations. Cassaine inhibited the
cholinesterase
activity of rat brain microsomes with a Ki of about 5 x 10(-5) M, but his inhibition was fully reversible. The poorly reversible inhibitory actions of cassaine, thus, appeared specific for Na+ + K+-ATPase. Because this stable pattern of inhibition of the Na+ + K+-ATPase by cassaine required drug concentrations at least one hundred-fold greater than those which produce positive inotropic effects, it appears unlikely that this pattern of Na+ + K+-ATPase inhibition is involved in the cardiotonic actions of this drug.
...
PMID:Studies on the stable inhibition of Na+ + K+-ATPase by cassaine. 13 Feb 44
Human erythrocytes from healthy male donors were fractionated with respect to in vivo age by simple centrifugation in order to characterize changes in the functional integrity of the membrane during the life-span of the cell. The three enzymes, Na/K-ATPase, glyceraldehyde-3-phosphate dehydrogenase and
NADH
-ferricyanide reductase, were found not to change with age, but significant age-dependent decreases were observed in the cases of
acetylcholinesterase
, phosphoglycerate kinase, purine nucleoside phosphorylase, adenylate kinase, Mg-ATPase and alkaline phosphatase. The possibility that these changes were attributable to mechanisms other than age-related inactivation, such as reticulocyte contamination, differential resealing and crypticity, was investigated. Only the decrease in
acetylcholinesterase
could be explained wholly in terms of reticulocyte contamination. A decrease in membrane integrity on ageing was observed, which accounted for approximately half the change in alkaline phosphatase and may have contributed to the other enzyme activity changes. This membrane integrity effect masked a real decrease in the highly cryptic
NADH
-ferricyanide reductase, this decrease being apparent only after total disaggregation of the membrane with nonionic surfactant.
...
PMID:Changes in the activities of some membrane-associated enzymes during in vivo ageing of the normal human erythrocyte. 14 40
Stereotaxic septal cannulation in one hemisphere of the rat results in displacement of the ipsilateral basal ganglion along its rostrocaudal axis. In an attempt to elucidate any metabolic changes in the ganglion due to possible alteration in its vascular supply in the displaced position, enzyme histochemical studies were undertaken on the forebrain of septally cannulated rats. A survey of hydrolases (acid and alkaline phosphatases, ATPase,
cholinesterase
and non-specific esterases), dehydrogenases (succinate and lactate) and diaphorases (
NADH
- and NADPH- tetrazolium reductases) revealed no difference in activity between the ganglia of the two sides. Cortical activity appeared to be enhanced with a rostral shift of the ganglion and decreased with a caudal shift. In the light of available histoenzymatic data on ischaemic brain damages, the present results rule out the existence of any major metabolic difference between the two basal ganglia. This underlines the extraordinary degree of functional plasticity of subcortical nuclear masses, despite considerable physical displacement.
...
PMID:Enzyme histochemistry of basal ganglia in the septally cannulated rat. 14 57
The phospholipid requirement of membrane-bound enzymes may depend on several reasons. In our laboratory we have investigated lipids (1) as a bidimensional medium required for the movement of Coenzyme Q, a lipid-soluble cofactor of the mitochondrial respiratory chain, and (2) as a hydrophobic environment necessary to impose the proper conformation to membrane-bound enzymic proteins. We have found that Coenzyme Q, once reduced by NADH dehydrogenase, must cross the inner mitochondrial membrane; only quinones having long isoprenoid side chains can easily cross phospholipid bilayers, and this is the reason why a short chain quinone such as CoQ-3 inhibits
NADH
oxidation. The incapability of short quinones to cross lipid bilayers is due to their disposition in the lipid bilayer, stacked within the phospholipids. The conformational role of lipids has been investigated indirectly observing the kinetics of membrane-bound enzymes, e.g. the mitochondrial ATPase, and directly by circular dichroism. Lipid removal or lipid perturbation with organic solvents induce a decrease of alpha-helical content in mitochondrial proteins, and give rise to a series of kinetic changes in ATPase, including uncompetitive inhibition, increased activation energy, and loss of cooperativity in oligomycin inhibition. The recognition of a conformational role of lipids has allowed us to postulate a working hypothesis for the mechanism of action of general anesthetics. Such drugs have been found by us, by means of spin labels and fluorescent probes, to disrupt lipid protein interactions in several membranes, including synaptic membranes. The loosening of such interactions is believed to induce conformational changes, which will alter ion transport systems necessary to the propagation of neural impulses. Conformational changes induced by anesthetics have been found by us both directly by circular dichroism and indirectly by enzyme kinetics. The conformational effect of anesthetics is not directly exerted on the proteins but is mediated through the lipids. In agreement with this hypothesis we have found that membrane-bound
acetylcholinesterase
is inhibited by anesthetics, whereas the solubilized enzyme is not inhibited. However, binding of the solubilized enzyme to phospholipids restores anesthetic inhibition.
...
PMID:Biophysical studies on agents affecting the state of membrane lipids: biochemical and pharmacological implications. 15 58
The enteric nerve plexuses of the domestic fowl (Gallus domesticus) were investigated in sections and stretch preparations by means of the
cholinesterase
and glyoxylic acid fluorescence histochemical techniques. Cholinesterase-positive and varicose and non-varicose fluorescent nerve fibers were distributed at all levels of the gut in myenteric, submucosal, muscle and mucosal plexuses, and in a perivascular plexus. The density of the innervation and the detailed distribution of the nerves varied in different parts of the intestinal tract. All nerve plexuses appeared to be best developed in the rectum. Whereas the circular muscle coat contained a substantial number of nerves at all levels of the gut, the longitudinal coat was well innervated only in the rectum. The major portion of the mucosal plexus appeared to be associated with the intestinal glands. The nerve cell bodies were restricted to the myenteric and submucosal plexuses and were mainly
cholinesterase
-positive. Fluorescent ganglion cells were not observed. Pretreatment of stretch preparations with
NADH
: Nitro BT to stain ganglion cells showed that the majority of the cells were surrounded by a meshwork of fluorescent varicose fibres, although none of the fibres appeared to be associated with individual cells. The perivascular plexus was mainly associated with the arteries. The functional significance of the innervation is discussed.
...
PMID:Avian enteric nerve plexuses. A histochemical study. 65 58
Sheep erythrocyte membranes have been shown in this laboratory to undergo spontaneous vesiculation when incubated at 4 degrees, fractionating into two bands in dextran gradients (R. McGuire and R. Barber, submitted for publication). While vesicles were observed to be formed in several solvent systems, incubation in the presence of complexors to remove divalent cations was found to be the most efficient method for both vesicle formation and their detachment from the residual membrane. We report here on the characterization of these vesicles formed by spontaneous vesiculation. In the presence of a hypotnoic buffer containing 1 mM EDTA, vesicle production proceeds linearly up to 50 hours and declines, reaching its maximum at 72 hours with up to 20% of the total membrane protein found in the upper band. This upper band is shown in electron micrographs to be composed chiefly of closed vesicles, while the particles in the lower band appear morphologically similar to the original ghosts. Total phospholipid phosphorus and cholesterol in the vesicles are enriched to the same extent, giving a lipid to protein ratio of 2 times that found for whole ghosts. The vesicles contain the same individual phospholipids as the ghosts. The protein composition of these vesicles is unique, in that they are almost depleted in the known extrinsic membrane proteins, while containing practically all types of the various glycoproteins of the original membrane. The two main intrinsic membrane proteins (with apparent molecular weights of 160,000 and 100,000) are found almost exclusively in the vesicles, virtually depleted in the residual ghost-like particles. The protein with 160,000 molecular weight is shown here to be a glycoprotein, giving an anomalous molecular weight on sodium dodecyl sulfate gels and having a molecular weight of approximately 50,000 after lipid extraction. This same glycoprotein appears to fractionate with
acetylcholinesterase
. From the accessibilities of the substrates to the membrane
acetylcholinesterase
and
NADH
-diaphorase, it is concluded that the vesicles are right-side-out and sealed to small molecules. There are more membrane sialic acid residues accessible to neuraminidase in the vesicles (in terms of number of residues/mg og membrane protein) than in ghosts, further supporting the conclustion that these vesicles have a normal orientation and are enriched in glycoproteins. The specific activity of
acetylcholinesterase
in the vesicles is increased 5- to 6-fold over that found in the original ghosts and almost 20-fold over that in the residual ghost-like particles. Consequently, spontaneous vesiculation occurs simultaneously with the enrichement of specific membrane proteins in certain regions of the lipid bilayer. It is postulated that these domains in the membrane, containing clusters of specific intrinsic membrane proteins, bud out and subsequently release glycoprotein-enriched lipid vesicles.
...
PMID:Glycoprotein-enriched vesicles from sheep erythrocyte ghosts obtained by spontaneous vesiculation. 93 96
The levels of acetylcholine and choline were measured in various brain regions of the rat after fixation by microwave irradiation of the head and after decapitation and subsequent freezing in liquid nitrogen. Levels of acetylcholine were increased by approximately 50% after microwave irradiation, while choline levels were reduced. These biochemical findings were correlated with virtually complex loss of
acetylcholinesterase
and
NADH
-diaphorase activity after 1 s exposure to microwave irradiation at a level of 5 kW.
...
PMID:Fast fixation of brain in situ by high intensity microwave irradiation: application to neurochemical studies. 104 75
Infusion of 1 mul arachis oil containing 1.5 mug bis-(1 -methylethyl)phosphorofluoridate (di-isopropylfluorophosphate: DFP) into the caudate--putamen nucleus and substantia nigra of rats produced a considerable reduction of histochemical staining for
acetylcholinesterase
(
AChE
) in these two brain regions 30--120 min after injection. Thereafter, regeneration of
AChE
occurred within the zone of DFP effect. These new stores of
AChE
were associated with discrete neuronal perikarya and their processes. Intracerebral DFP administration had little or no histochemically detectable effect on
NADH
-diaphorase. Thionin staining was similarly unaffected. The results with punctate intracerebral application of DFP were replicated by intramuscular injection of 1.5 mg/kg DFP. Although the significance of dopaminergic--cholinergic interactions in the neostriatum could not be elucidated on the basis of these histochemical data, the thesis was advanced that dopamine neurons in the pars compacta of the substantia nigra also contained
AChE
, possibly to inactivate acetylcholine released from cholinergic fibers afferent to this neural structure.
...
PMID:Acetylcholinesterase-containing neurons in the neostriatum and substantia nigra revealed after punctate intracerebral injection of di-isopropylfluorophosphate. 123 57
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