Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The objective of this study was to determine if biocytin would reliably label details of distant axons and dendrites when injected extracellularly in primates. Biocytin (2.5-5%) was injected iontophoretically or by pressure into several areas of the visual and somatosensory systems of macaque monkeys, squirrel monkeys, tree shrews and galagos. After survival times that ranged from 9 h to 2 weeks, fine details of anterogradely filled axons and/or retrogradely filled dendrites were reliably revealed with an avidin-biotin-HRP complex (ABC solution) that was enhanced with heavy metals. Biocytin labeling was successfully combined with choline acetyltransferase (ChAT) or cytochrome oxidase (CO) histochemistry to reveal double-labeled cells. Our results show that biocytin is a versatile, easy-to-use label that completely fills cell processes both anterogradely and retrogradely in several primate species.
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PMID:Morphological details of primate axons and dendrites revealed by extracellular injection of biocytin: an economic and reliable alternative to PHA-L. 172 35

Bioenergetics of the aerobic bacteriochlorophyll a-containing (BCl a) bacterium (ABC bacterium) Roseinatronobacter thiooxidans is a combination of photosynthesis, oxygen respiration, and oxidation of sulfur compounds under alkaliphilic conditions. The photosynthetic activity of Rna. thiooxidans cells was established by the photoinhibition of cell respiration and reversible photobleaching discoloration of the BCl a of reaction centers (RC), connected by the chain of electron transfer with cytochrome c551 oxidation. The species under study, like many purple bacteria and some of the known ABC bacteria, possesses a light-harvesting pigment-protein (LHI) complex with the average number of 30 molecules of antenna BCl a per one photosynthetic RC. Under microaerobic growth conditions, the cells contained bc1 complex and two terminal oxidases: cbb3-cytochrome oxidase and the alternative cytochrome oxidase of the a3 type. Besides, Rna. thiooxidans was shown to have several different soluble low- and high-potential cytochromes c, probably associated with the ability of utilizing sulfur compounds as additional electron donors.
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PMID:[Photosynthetic activity and components of the electron transport chain in the aerobic bacteriochlorophyll A-containing bacterium Roseinatronobacter thiooxidans]. 1933 93

Cytochrome c oxidase or mitochondrial respiratory chain complex IV is where over 90% of oxygen is consumed. The relationship between complex IV activity and mitochondrial proteins, which provides a guide to understanding the mechanisms in primary mitochondrial disorders, has been determined by histochemistry (activity) and immunohistochemistry in serial sections. In the central nervous system (CNS), mitochondrial activity and immunoreactivity have been determined in populations of cells in serial sections as capturing cells in more than one section is difficult. In this report we describe a method to determine complex IV activity in relation to mitochondrial proteins at a single cell level in the CNS. We performed complex IV histochemistry and immunohistochemistry consecutively in snap frozen sections. Although the product of complex IV histochemistry reduces the sensitivity of standard immunohistochemistry (secondary antibody and ABC method) the biotin-free Menapath polymer detection system (A. Menarini Diagnostics, Wokingham, UK) enables mitochondrial proteins to be detected following complex IV histochemistry. The co-occurring chromogens may then be separately visualised and analysed using multi-spectral imaging (Nuance system CRi, Woburn, MA). Our technique is applicable for exploring mitochondrial defects within single cells in a variety of CNS disorders and animal models of those diseases.
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PMID:Detection of cytochrome c oxidase activity and mitochondrial proteins in single cells. 1972 40

Cytochrome c oxidase or mitochondrial respiratory chain complex IV is where over 90% of oxygen is consumed. The relationship between complex IV activity and mitochondrial proteins, which provides a guide to understanding the mechanisms in primary mitochondrial disorders, has been determined by histochemistry (complex IV activity) and immunohistochemistry in serial sections. In the central nervous system (CNS), mitochondrial activity and immunoreactivity have been determined in populations of cells in serial sections as capturing cells in more than one section is difficult. In this report, we describe a method to determine complex IV activity in relation to mitochondrial proteins at a single-cell level in the CNS. We performed complex IV histochemistry and immunohistochemistry consecutively in snap-frozen sections. Although the product of complex IV histochemistry reduces the sensitivity of standard immunohistochemistry (secondary antibody and ABC method), the biotin-free Menapath polymer detection system enables mitochondrial proteins to be detected following complex IV histochemistry. The co-occurring chromogens may then be separately visualized and analyzed using multispectral imaging. Our technique is applicable for exploring mitochondrial defects within single cells, including oligodendrocytes, in a variety of CNS disorders and animal models of those diseases.
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PMID:A Method to Detect Cytochrome c Oxidase Activity and Mitochondrial Proteins in Oligodendrocytes. 3082 Sep 8