scholarly journals Binding of 1,1,1-trichloro-2,2-di-p-chlorophenylethane (DDT) with subcellular fractions of rat brain

1969 ◽  
Vol 114 (1) ◽  
pp. 135-139 ◽  
Author(s):  
Hans Brunnert ◽  
Fumio Matsumura
Keyword(s):  
Rat Brain ◽  
Nerve Ending ◽  
Soluble Proteins ◽  
Subcellular Fractions ◽  
Nerve Endings ◽  
Sephadex Column ◽  
Column Method ◽  
Synaptic Complexes ◽  
Soluble Components

DDT (1,1,1-trichloro-2,2-di-p-chlorophenylethane) and DDE (1,1-dichloro-2,2-di-p-chlorophenylethylene, a non-insecticidal analogue of DDT) were found to bind with various nerve components of rat brain. The amount of DDT binding exceeded that of DDE only in the fraction containing mainly the nerve endings. Among various components in the nerve-ending fraction, a subfraction containing mainly the pre- and post-synaptic complexes had the highest affinity for DDT in comparison with that for DDE. By using an ‘acetone-powdering’ technique on brain preparations, the Sephadex-column method was shown to provide reliable results for studies on the binding of DDT or DDE with soluble proteins in the nerve tissues. From these results it was concluded that DDE had a higher affinity for soluble components of the rat brain than did DDT.

Histochemical and Biochemical Demonstration of Sialic Acid and Sulphate in Vesicles and Membranes Isolated from Nerve Endings of Rat Brain

1973 ◽  
Vol 13 (1) ◽  
pp. 237-255
Author(s):  
RUTH MARX ◽  
ELKE GRAF ◽  
W. WESEMANN
Keyword(s):  
Sialic Acid ◽  
Rat Brain ◽  
Sulphuric Acid ◽  
Nerve Ending ◽  
Synaptic Vesicles ◽  
Iron Hydroxide ◽  
Acid Methyl Ester ◽  
Nerve Endings ◽  
Uniform Size ◽  
Colloidal Iron

The reaction of colloidal iron hydroxide (CIH) with acidic groups was applied for an ultra-structural study of the distribution of sulphuric acid monoesters and sialic acid in synaptic vesicles and external nerve ending membranes isolated from rat brain. At pH 1.7 CIH was precipitated as electron-dense granules with a uniform size of 6-7 nm specifically labelling the carboxyl group of sialic acid and the sulphate group of monoesters of sulphuric acid. The differentiation of these 2 groups was achieved by treatment with neuraminidase and methylation followed by saponification. After preincubation with neuraminidase, which released 90-100% of the sialic acid from the membranes of the synaptic vesicles and the nerve endings, the electron-dense deposits marked the reaction sites of sulphate with CIH. The sulphate groups which were present at a concentration of 2.3 and 2.2 µmol/mg protein for the synaptic vesicle and nerve ending membrane preparations, respectively, were rendered soluble as methyl monosulphate by trans-esterification with acid/methanol and quantitatively removed from the structures. By this treatment membrane-bound sialic acid was blocked as sialic acid methyl ester and partly split off by acid hydrolysis. About 55% of the sialic acid found in the nerve ending membranes remained attached to the structure as compared with about 35% of the sialic acid of the vesicles. The acid-resistant proportion of the sialic acid could be localized with CIH after saponification of the esterified preparations. The method described allows the electron-microscopical demonstration of acid-resistant, neuraminidase-sensitive sialic acid in synaptic structures and the discrimination from sulphated mucopolysaccharides.

scholarly journals [3H]2-(4-Phenylpiperidino)cyclohexanol (AH5183) binding to synaptosomes and subcellular fractions obtained from rat brain

1993 ◽  
Vol 157 (1) ◽  
pp. 72-74 ◽  
Author(s):  
Takeshi Suzuki ◽  
Yuko Kashima ◽  
Kazuko Fujimoto ◽  
Koichiro Kawashima
Keyword(s):  
Rat Brain ◽  
Subcellular Fractions

LOCALIZATION AND CHARACTERIZATION OF CHOLINESTERASE IN SUBCELLULAR FRACTIONS OF RAT BRAIN AND BEEF PITUITARY

1961 ◽  
Vol 39 (9) ◽  
pp. 1335-1345 ◽  
Author(s):  
Surendra S. Parmar ◽  
Morley C. Sutter ◽  
Mark Nickerson
Keyword(s):  
Rat Brain ◽  
Cholinesterase Activity ◽  
Succinic Dehydrogenase ◽  
Anterior Lobe ◽  
Subcellular Fractions ◽  
Posterior Pituitary ◽  
Low Concentrations ◽  
Pituitary Glands ◽  
Hydrolysis Of

Fresh rat brains and fresh anterior and posterior pituitary glands of beef were separated by differential centrifugation into subcellular fractions, characterized on the basis of sedimentation and succinic dehydrogenase activity. Cholinesterase activity was measured by both manometric and colorimetric methods, the results of which were comparable. Cholinesterase activity of rat brain was found mainly in the microsome and supernatant fractions. It was quite uniformly distributed in all subcellular fractions of both anterior and posterior pituitary. Comparisons of the relative rates of hydrolysis of acetylthiocholine and butyrylthiocholine, and of inhibition by eserine, indicated that brain contains a much higher percentage of acetylcholinesterase than do both lobes of the pituitary, which contain relatively low concentrations of the specific enzyme. Total cholinesterase activity and its sensitivity to inhibition by eserine in the posterior pituitary were found to be midway between those of the anterior lobe and of the brain, from which the posterior pituitary was derived during embryological development.

Evaluation of rat brain subcellular fractions for the prediction of in vivo drug metabolism in brain

2018 ◽  
Vol 33 (1) ◽  
pp. S79 ◽  
Author(s):  
Mohammad Shadid ◽  
Ying Liu ◽  
Elvana Veizaj ◽  
Jiansheng Huang ◽  
Josh Johnson ◽  
...  
Keyword(s):  
Drug Metabolism ◽  
Rat Brain ◽  
Subcellular Fractions ◽  
In Vivo Drug Metabolism
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