دورية أكاديمية

Cholinesterase activity in the rat superior cervical ganglion: effect of denervation and axotomy.

التفاصيل البيبلوغرافية
العنوان: Cholinesterase activity in the rat superior cervical ganglion: effect of denervation and axotomy.
المؤلفون: Viana GB, Kauffman FC
المصدر: Brain research [Brain Res] 1984 Jun 18; Vol. 304 (1), pp. 37-45.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
اللغة: English
بيانات الدورية: Publisher: Elsevier/North-Holland Biomedical Press Country of Publication: Netherlands NLM ID: 0045503 Publication Model: Print Cited Medium: Print ISSN: 0006-8993 (Print) Linking ISSN: 00068993 NLM ISO Abbreviation: Brain Res Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Amsterdam Elsevier/North-Holland Biomedical Press.
مواضيع طبية MeSH: Nerve Regeneration* , Synaptic Transmission*/drug effects, Acetylcholinesterase/*metabolism , Axons/*enzymology , Butyrylcholinesterase/*metabolism , Cholinesterases/*metabolism , Ganglia, Sympathetic/*enzymology, Animals ; Autonomic Fibers, Postganglionic/enzymology ; Autonomic Fibers, Preganglionic/enzymology ; Cholinesterase Inhibitors/pharmacology ; Chromatography, Gel ; Denervation ; Ganglia, Sympathetic/drug effects ; Isoenzymes/metabolism ; Male ; Molecular Weight ; Rats ; Rats, Inbred Strains
مستخلص: Cholinesterase activity and its various forms in the superior cervical ganglion of the rat were studied after denervation, axotomy and double section. The response of this activity to various inhibitors was also studied. The specific activity of cholinesterase activity was 323 +/- 25 nmol/mg protein/min in homogenates of normal ganglia and the total enzyme activity was 78 +/- 5 nmol/ganglion/min. Axotomy produced approximately a 40% decrease in total activity in ganglia at 3 days compared to contralateral ganglia. Activity in the contralateral ganglia was also decreased by about 30% compared to normal ganglia. Decentralization alone for 3 days did not affect the specific or total cholinesterase activity. However, decentralization followed by axotomy 3 days later resulted in a greater loss in activity compared to axotomy and a significant change in the forms of cholinesterase. After chromatography on Sepharose 6B-100 columns, 3 forms (a, c, d) of cholinesterase activity could be separated from homogenates of single ganglia. The 3 forms had estimated molecular weights of 1,934,000, 129,000 and 59,000 daltons, respectively. A fourth form (b) presented as a shoulder and had an estimated molecular weight of 404,000 daltons. Decentralization or axotomy decreased forms a and d. A reduction in the proportion of form c was also observed in the axotomized ganglion. Decentralization followed by axomoty resulted in large decreases in forms a, b and c and complete loss of form d. Assay of the separated forms in the presence of the specific inhibitor of acetylcholinesterase, BW284C-51, indicated that the majority of the enzyme recovered after chromatography is acetylcholinesterase.
معلومات مُعتمدة: HD 16596 United States HD NICHD NIH HHS
المشرفين على المادة: 0 (Cholinesterase Inhibitors)
0 (Isoenzymes)
EC 3.1.1.7 (Acetylcholinesterase)
EC 3.1.1.8 (Butyrylcholinesterase)
EC 3.1.1.8 (Cholinesterases)
تواريخ الأحداث: Date Created: 19840618 Date Completed: 19840912 Latest Revision: 20190614
رمز التحديث: 20240627
DOI: 10.1016/0006-8993(84)90859-x
PMID: 6331583
قاعدة البيانات: MEDLINE
الوصف
تدمد:0006-8993
DOI:10.1016/0006-8993(84)90859-x