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Microscopical localization of adenylate cyclase: A historical review of methodologies
Author(s) -
Richards P.A.,
Richards P.D.G.
Publication year - 1998
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/(sici)1097-0029(19980301)40:6<434::aid-jemt2>3.0.co;2-p
Subject(s) - adenylate kinase , cyclase , computational biology , computer science , biology , chemistry , biochemistry , enzyme
The histochemistry technique for localizing adenylate cyclase has been developed over the past two decades. Early efforts were directed at overcoming the criticism of the lead capture technique, the inhibition of the enzyme by fixation, and problems associated with the substrate. The introduction of alternative metal ions, strontium and cerium, offered solutions to the criticism of the lead capture technique. The inhibition of the enzyme by the various fixation methods used has been rarely overcome satisfactorily and the use of non‐fixed material during incubation is one of the alternatives that has been suggested. The introduction of adenylate (β‐γ‐methylene) diphosphate as an alternative substrate offers a solution to the problems associated with commercially available adenylyl imidodiphosphate. Although no standard medium or method has been accepted by all researchers, the histochemical technique still has a place in the arsenal of the modern cell biologist. The technique localizes the active enzyme, as opposed to the protein, active and nonactive, by immunocytochemistry and the precursors of the protein by in situ hybridization methods. Microsc. Res. Tech. 40:434–439, 1998. © 1998 Wiley‐Liss, Inc.