Renaissance of cytochemical localization of membrane ATPases in the myocardium

Author(s):  
Ján Slezák ◽  
Ludmila Okruhlicová ◽  
Narcisa Tribulová ◽  
Wolfgang Schulze ◽  
Naranjan S. Dhalla
1995 ◽  
Vol 147 (1-2) ◽  
pp. 169-172 ◽  
Author(s):  
J�n Slez�k ◽  
Ludmila Okruhlicov� ◽  
Narcisa Tribulov� ◽  
Wolfgang Schulze ◽  
Naranjan S. Dhalla

Author(s):  
W. A. Shannon ◽  
M. A. Matlib

Numerous studies have dealt with the cytochemical localization of cytochrome oxidase via cytochrome c. More recent studies have dealt with indicating initial foci of this reaction by altering incubation pH (1) or postosmication procedure (2,3). The following study is an attempt to locate such foci by altering membrane permeability. It is thought that such alterations within the limits of maintaining morphological integrity of the membranes will ease the entry of exogenous substrates resulting in a much quicker oxidation and subsequently a more precise definition of the oxidative reaction.The diaminobenzidine (DAB) method of Seligman et al. (4) was used. Minced pieces of rat liver were incubated for 1 hr following toluene treatment (5,6). Experimental variations consisted of incubating fixed or unfixed tissues treated with toluene and unfixed tissues treated with toluene and subsequently fixed.


Author(s):  
Judith A. Murphy ◽  
Mary R. Thompson ◽  
A.J. Pappelis

In an attempt to identify polysaccharide components in thin sections of D. maydis, procedures were employed such that a PAS localization could be carried out. Three different fixatives were evaluated ie. glutaraldehyde, formaldehyde and paraformaldehyde. These were used in conjunction with periodic acid (PA), thiosemicarbazide(TSC), and osmium tetroxide(Os) to localize polysaccharides in V. maydis using a pre-embedded reaction procedure. Polysaccharide localization is based on the oxidation of vic-glycol groups by PA, and the binding of TSC as a selective reaction center for the formation of osmium black. The reaction product is sufficiently electron opaque, insoluble in lipids, not altered when tissue is embedded, and has a fine amorphous character.


2013 ◽  
Vol 154 (3) ◽  
pp. 387-395 ◽  
Author(s):  
Elmouldi Garoui ◽  
Ibtissem Ben Amara ◽  
Dorra Driss ◽  
Awatef Elwej ◽  
Semia Ellouze Chaabouni ◽  
...  

1972 ◽  
Vol 20 (11) ◽  
pp. 873-879 ◽  
Author(s):  
S. L. HOWELL ◽  
MARGARET WHITFIELD

A cytochemical method has been used to investigate the localization of adenyl cyclase activity in A and B cells of isolated rat islets of Langerhans. Adenosine triphosphate was initially utilized as substrate, the pyrophosphate liberated being precipitated by lead ions at its site of production. The specificity of the method was increased by the use of adenylyl-imidodiphosphate as an alternative substrate; this adenosine triphosphate analogue was not hydrolyzed by adenosine triphosphatase but provided an effective substrate for adenyl cyclase. Adenyl cyclase activity, which was found to retain its glucagon and fluoride sensitivity in glutaraldehyde-fixed tissue, was found exclusively and almost uniformly in the plasma membranes of A and B cells. Storage granule membrane, incorporated into the plasma membrane during secretion of the granule content by exocytosis, appeared to be devoid of adenyl cyclase activity.


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