QUANTITATIVE CHARACTERIZATION OF A HISTOCHEMICAL ENZYME SYSTEM
نویسندگان
چکیده
منابع مشابه
a study on construction of iranian life tables: the case study of modified brass logit system
چکیده ندارد.
15 صفحه اولHistochemical method for characterization of enzyme crystals: application to crystals of Torpedo californica acetylcholinesterase.
Histochemical methods are employed to detect and localize a wide range of enzymes. Even though protein crystallographers do not commonly use this technique, the extensively used colorimetric reaction of Karnovsky was successfully adapted for easy and quick identification of acetylcholinesterase crystals. The method relies on the reduction of ferricyanide to ferrocyanide by thiocholine, released...
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A novel technique combining the freeze drying and embedding in glycol methacrylate at low temperature of tissue permitted the histochemical demonstration of a variety of enzymes, showing maintenance of enzyme activity, accurate enzyme localisation without apparent diffusion, and excellent morphological detail. The results obtained with this new approach were superior to standard techniques used...
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Histochemical observations were carried out on various hydrolytic enzymes in the spontaneous mammary carcinoma of C3H-strain mice. Alkaline phosphatase activity was observed in the luminal border of the tubular structure and in the periluminal surface, which showed a cystic dilatation in ducts and papillae. Capillaries in the stroma showed a high enzymatic activity. Acid phosphatase activity wa...
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BACKGROUND Cardiac conduction is influenced by peptidergic mechanisms as well as classic neurotransmitters. The distribution of peptide-containing nerves has not been well defined. METHODS AND RESULTS Immunofluorescence and histochemical techniques were used to visualize the innervation of the human conduction system and to distinguish nerve subpopulations according to their peptide and enzym...
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ژورنال
عنوان ژورنال: Journal of Histochemistry & Cytochemistry
سال: 1964
ISSN: 0022-1554,1551-5044
DOI: 10.1177/12.5.315