Stabilization of configurational states and enzyme activities in subcellular fractions after fixation with extremely low concentrations of glutaraldehyde.
Histochem J, 1976/3;8(2):113-20.
Asano M, Kurono C, Wakabayashi T, Kimura H
PMID: 178635
Abstract
The activities of various enzymes in some subcellular organelle fractions were examined after fixation in glutaraldehyde of various concentrations. A high speed centrifuge was used to shorten the fixation time. At the lowest concentration (0.01%) glutaraldehyde stabilized instable configurational states of mitochondria as revealed by electron microscopy. In addition, at this concentration, at least 70% of the original monoamine oxidase, ATPase and cytochrome oxidase activities were preserved. The activity of acid phosphatase, on the other hand, was enhanced in a lysosomal fraction when fixed with the aldehyde at higher concentrations, e.g. 0.1% and 1.0%. It is possible that the aldehyde at higher concentrations has the same effects on the lysosomal membrane as freeze-thawing. Glucose-6-phosphatase activity was well-preserved in a microsomal fraction fixed with 0.01% glutaraldehyde but was decreased drastically when the concentration of the aldehyde was greater than 0.05%.
MeSH terms
Adenosine Triphosphatases; Animals; Cattle; Dinitrophenols; Electron Transport Complex IV; Enzyme Activation; Histocytochemistry; Lysophosphatidylcholines; Magnesium; Male; Microscopy, Electron; Mitochondria, Liver; Mitochondria, Muscle; Monoamine Oxidase; Myocardium; Rats
More resources
EndNote: Download