The Histochemical journal, 12(1), 71-86 (1980-01-01)
Using the substrate 2-naphthylthiol acetate (NTA), we developed a reproducible method of demonstrating a non-specific esterase while retaining nuclear and cytoplasmic details at the ultrastructural level. The NTA esterase had a distribution and pattern of staining similar to those of
1- and 2-thionaphthylacetates were tested as cholinesterase substrates. It was shown that the butyrilcholinesterase from horse serum can hydrolize these compounds. The hydrolysis velocity of 1-thionaphthylacetate was comparable with hydrolysis velocity of acetylthiocholine (the well known cholinesterase substrate), but 2-thionaphthylacetate
Experimental and molecular pathology, 46(3), 321-330 (1987-06-01)
Nonspecific esterase activity was localized ultrastructurally within normal and leukemic hematopoietic cells by the use of 2-naphthylthiol acetate (NTA) as a substrate. NTA esterase activity was identified in all cell lines, although mononuclear phagocytes contained the most abundant activity. Monocytes
The Histochemical journal, 17(1), 43-56 (1985-01-01)
A 2-thionaphthyl acetate substrate was utilized to assess the subcellular distribution of nonspecific esterases in rat pulmonary alveolar and peritoneal macrophages. The enzymatically liberated 2-thionaphthol was visualized at pH 7.1 by utilizing gold as a capture agent. Glutaraldehyde-fixed macrophages derived
Questions
Reviews
★★★★★ No rating value
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.