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cochlearia/lisina
L'enllaç es desa al porta-retalls
4 resultats
Double labeling of neural circuits using horseradish peroxidase and cobalt.
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This describes for the first time a non-fluorescent method for studying the connectional interrelationship of two neuronal systems in the same histological sections in which the systems are stained in two different colors (blue and brown). Since HRP and cobaltous-lysine are transported in both
Distal and proximal ligand interactions in heme proteins: correlations between C-O and Fe-C vibrational frequencies, oxygen-17 and carbon-13 nuclear magnetic resonance chemical shifts, and oxygen-17 nuclear quadrupole coupling constants in C17O- and 13CO-labeled species.
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We have obtained the oxygen-17 nuclear magnetic resonance (NMR) spectra of a variety of C17O-labeled heme proteins, including sperm whale (Physeter catodon) myoglobin, two synthetic sperm whale myoglobin mutants (His E7----Val E7; His E7----Phe E7), adult human hemoglobin, rabbit (Oryctolagus
Histochemical localization of cytochrome oxidase in the retina and optic tectum of normal goldfish: a combined cytochrome oxidase-horseradish peroxidase study.
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Cytochrome oxidase (C.O.) was histochemically localized in the normal retina and optic tectum of goldfish in order to examine the laminar and cellular oxidative metabolic organization of these structures. In the optic tectum, C.O. exhibited a distinct laminar, regional, and cellular distribution.
Tubular inhibition destroys charge selectivity for anionic and neutral horseradish peroxidase.
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The fractional clearance of [3H]anionic HRP and [3H]neutral HRP in the isolated perfused kidney as determined by radioactivity analysis was 0.0160+/-0.0028 (n=6) and 0.0388+/-0.0076 (n=8) respectively. The apparent charge selectivity for both the anionic and neutral forms of HRP observed was
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