PROBLEMS OF LIGHT MICROSCOPICAL ADENYLATE CYCLASE DEMONSTRATION IN RAT CEREBELLUM WITH ADENYLYL IMIDODIPHOSPHATE

Adenylate cyclase in rat cerebellum was investigated on the light microscopic level with adenylyl imidodiphosphate (AMP-PNP) as substrate. The results show that the reaction is overlapped by other enzymes with high activity and inhibited by NaF and dithiothreitole. It does not seem possible to demon...

Full description

Saved in:

Bibliographic Details
Published in:	ACTA HISTOCHEMICA ET CYTOCHEMICA Vol. 17; no. 5; pp. 603 - 611
Main Authors:	POEGGEL, GERD, LUPPA, HANS
Format:	Journal Article
Language:	English
Published:	Kyoto JAPAN SOCIETY OF HISTOCHEMISTRY AND CYTOCHEMISTRY 01-01-1984 Japan Society of Histochemistry and Cytochemistry Japan Science and Technology Agency
Subjects:	adenylate cyclase Biochemistry and metabolism Biological and medical sciences Central nervous system cerebellum Fundamental and applied biological sciences. Psychology rats staining Vertebrates: nervous system and sense organs Cerebellum Adenylate cyclase Vertebrata Mammalia Rat Enzyme Rodentia Central nervous system Brain (Vertebrata) Histochemistry
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	Adenylate cyclase in rat cerebellum was investigated on the light microscopic level with adenylyl imidodiphosphate (AMP-PNP) as substrate. The results show that the reaction is overlapped by other enzymes with high activity and inhibited by NaF and dithiothreitole. It does not seem possible to demonstrate adenylate cyclase light microscopically in rat cerebellum because adenylate cyclase activators inhibit the conversion of AMP-PNP. The biochemical results of Johnson and Welden (7) could be confirmed histochemically.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23
ISSN:	0044-5991 1347-5800
DOI:	10.1267/ahc.17.603