Results 91 to 100 of about 4,040 (119)

Ending remarks from the CANPS chair

2010 17th IEEE-NPSS Real Time Conference, 2010
The 17th IEEE Real Time Conference (RT10) took place on May 23–28 at the heart of Lisbon, Portugal, in the Instituto Superior Tecnico in Lisbon. It was organized by the Instituto de Plasmas e Fusoo Nuclear (IPFN) together with the Laboratorio de Instrumentacoo e Fisica Experimental de Particulas (LIP).
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Investigations on spectroscopic and elasticity studies of Nd2O3 doped CANP phosphate glasses

Journal of Alloys and Compounds, 2017
Quaternary phosphate glasses CoO - Al2O3 - Na2O - P2O5 (CANP) doped with – different concentrations of Nd2O3 had prepared and studied by FTIR, ultrasonic parameters and UV–Vis–NIR techniques. The Judd-Ofelt theory has applied to describe the absorption and luminescence spectra of Nd3+ ions in these glasses.
Yasser B. Saddeek, A.A. El-Maaref, K.A. Aly, M.M. ElOkr, A.A. showahy   +4 more
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Calcium-activated neutral protease (CANP) in normal and dysmyelinating mutant paralytic tremor rabbit myelin

Molecular and Chemical Neuropathology, 1992
Calcium-activated neutral protease (CANP) in normal and dysmyelinating mutant, paralytic tremor (PT) rabbit myelin and premyelin fractions was studied using immature (4-5 wk) or adult animals. The enzyme was estimated by determination of its catalytic activity as well as by using immunoblot analysis after SDS-PAGE separation.
K, Domańska-Janik, B, de Nechaud, M, Inomata, S, Kawashima, T, Zalewska   +4 more
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Limited Autolysis of Ca2+-Activated Neutral Protease (CANP) Changes Its Sensitivity to Ca2+ Ions

The Journal of Biochemistry, 1981
Ca2+-activated neutral protease (CANP) usually requires mM Ca2+ for activation. The sensitivity of CANP to Ca2+ is greatly enhanced by passing it through a casein-Sepharose column in the presence of Ca2+ ions. This conversion is ascribed to autolysis of CANP. The converted enzyme required 40 microM Ca2+ for 50% activation.
K, Suzuki, S, Tsuji, S, Kubota, Y, Kimura, K, Imahori   +4 more
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Immunohistochemical distribution of calcium‐activated neutral proteinases and endogenous CANP inhibitor in the rabbit hippocampus

Journal of Comparative Neurology, 1990
AbstractIntracellular accumulation of Ca2+ after brain ischemia is regarded as one of the principal causes of neuronal death, but details of the intracellular events occurring after Ca2+ accumulation have not yet been described. We propose that a calcium‐activated neutral proteinase which can degrade neuronal cytoskeletal proteins might link Ca2 ...
T, Fukuda, E, Adachi, S, Kawashima, I, Yoshiya, P H, Hashimoto   +4 more
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Calcium-Activated Neutral Protease (CANP) and its Biological and Medical Implications

1987
Calcium activated neutral protease (CANP) apparently participates in a variety of cellular functions mediated by Ca2 +. The primary, structure of CANP reveals a novel domain structure comprising domains highly homologous to papain-like cysteine proteinases and calmodulin-like Ca2+ binding proteins, and a glycine-rich hydrophobic domain that interacts ...
Koichi Suzuki, Shigeo Ohno, Yasufumi Emori, Shinobu Imajoh, Hiroshi Kawasaki   +4 more
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Purification of calcium-activated neutral proteinase (CANP) from purified myelin of bovine brain white matter

Neurochemical Research, 1988
A calcium-activated neutral proteinase was purified from myelin of bovine brain white matter. Myelin purified in the presence of EDTA (2 mM) was homogenized in 50 mM Trisacetate buffer at pH 7.5, containing 4 mM EDTA, 1 mM NaN3, 5 mM beta-mercaptoethanol and 0.1% Triton X-100 for two hours.
A K, Chakrabarti, N L, Banik
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Calcium-activated neutral protease (CANP), a putative processing enzyme of the neuropeptide, kyotorphin, in the brain

Biochemical and Biophysical Research Communications, 1988
Kyotorphin (Tyr-Arg) accumulation in the dialysed synaptosol from the rat brain in the presence of an inhibitor of kyotorphin-degrading enzyme, was maximal at neutral pH. This accumulation was activated by calcium ions, but was inhibited by leupeptin and SH-blocking agents, a finding which suggests the involvement of calcium-activated neutral protease (
Y, Yoshihara, H, Ueda, S, Imajoh, H, Takagi, M, Satoh   +4 more
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Localization and inhibition of calcium-activated neutral protease (CANP) in primate skeletal muscle and peripheral nerve

Experimental Neurology, 1987
Localization of calcium-activated neutral protease in normal monkey (Cebus apella) skeletal muscle and peripheral nerve was studied by application of the indirect immunofluorescent and peroxidase-antiperoxidase techniques for light and electron microscopy.
M A, Badalamente, L C, Hurst, A, Stracher   +2 more
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Effects of dibutyryl-cANP on glycolysis in washed human erythrocytes.

Acta biologica et medica Germanica, 1982
The experiments were carried out with washed human erythrocytes in order to study the effects of dibutyryl-cAMP (DB-cAMP) on glycolysis. 5 mM DB-cAMP significantly increases glucose consumption and lactate production in incubated erythrocytes. The cross-over plot of glycolytic intermediates shows that increased glycolysis is probably the result of ...
R, Zivković, M, Kostić, L, Mojsilović
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