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Clinica Chimica Acta, 1986
Calcium activated neutral protease (milli- and micro-forms) and its endogenous inhibitor have been quantified in muscle from Duchenne muscular dystrophy (DMD) patients. The specific activities of both the enzymes are found to be significantly elevated.
P A, Reddy +2 more
exaly +3 more sources
Calcium activated neutral protease (milli- and micro-forms) and its endogenous inhibitor have been quantified in muscle from Duchenne muscular dystrophy (DMD) patients. The specific activities of both the enzymes are found to be significantly elevated.
P A, Reddy +2 more
exaly +3 more sources
Specificity of calcium-activated neutral proteinase (CANP) inhibitors for human ?CANP and mCANP
Neurochemical Research, 1993We investigated the relative inhibition of purified human mu CANP and mCANP by five cysteine proteinase inhibitors including N-acetyl-Leu-Leu-nor-leucinal (C-I) and N-acetyl-Leu-Leu-methioninal (C-II), calpeptin, E64, and leupeptin. Based on IC50 measurements, calpeptin and C-I were stronger inhibitors by one to two orders of magnitude than C-II ...
Ralph A Nixon
exaly +3 more sources
Regulation of the calcium-activated neutral proteinase (CANP) of bovine brain by myelin lipids
BBA - Proteins and Proteomics, 1990Since calcium-activated neutral proteinase (CANP; calpain) activation occurs at the plasmalemma and the enzyme is found in myelin, we examined myelin lipid activation of brain CANP. Purified lipids were dried, sonicated and incubated with purified myelin CANP. The CANP was assayed using [14C]azocasein as substrate and the Ca2+ concentration ranged from
Somsankar Dasgupta, Naren Banik
exaly +5 more sources
Localization of calcium-activated neutral protease (CANP) in the peripheral nerve
Muscle and Nerve, 1985AbstractLocalization of calcium‐activated neutral protease (CANP) in the rat peripheral nerve was studied by an indirect immunofluorescent method, using rabbit antiserum against CANP extracted from chicken skeletal muscle. Its specificity to CANP, as well as its cross‐reactivity with rat CANP, were confirmed by the Ouchterlony immunodiffusion procedure
K, Kamakura +4 more
exaly +3 more sources
Hydrolysis of Protamine by Calcium-Activated Neutral Protease (CANP)
Journal of Biochemistry, 1985To determine the substrate recognition mechanism in calcium-activated neutral protease (CANP), the hydrolytic velocities for some possible substrates were compared. In general, succinylated polypeptides were poorer substrates than unmodified ones, suggesting that CANP interacts with positively charged amino groups and/or repels negatively charged ...
M, Hayashi +4 more
exaly +3 more sources
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.
Krystyna Domanska-Janik, Teresa Zalewska
exaly +3 more sources
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.
Krystyna Domanska-Janik, Teresa Zalewska
exaly +3 more sources
Life Sciences, 1987
The activity of calcium-activated neutral proteinase (mM CANP) was determined in homogenate, myelin and supernatant of bovine brain corpus callosum. The enzyme activity in homogenate and myelin was increased eleven and thirteen-fold respectively by Triton X-100.
Naren Banik
exaly +3 more sources
The activity of calcium-activated neutral proteinase (mM CANP) was determined in homogenate, myelin and supernatant of bovine brain corpus callosum. The enzyme activity in homogenate and myelin was increased eleven and thirteen-fold respectively by Triton X-100.
Naren Banik
exaly +3 more sources
Calcium-activated neutral protease (CANP) in brain and other tissues
Progress in Neurobiology, 1984U J, Zimmerman, W W, Schlaepfer
exaly +3 more sources
Journal of Neurochemistry, 1990
Abstract: We examined ganglioside modulation of the activity of the millimolar Ca2+‐sensitive form (mCANP) of calcium‐activated neutral proteinase (CANP), which is enriched in myelin, from brain. GM1, GD1a, GT1a, GM2, and GM4 produced a concentration‐dependent increase of mCANP activity. GD1a stimulated the greatest increase of enzyme activity (107%),
A K, Chakrabarti +3 more
openaire +2 more sources
Abstract: We examined ganglioside modulation of the activity of the millimolar Ca2+‐sensitive form (mCANP) of calcium‐activated neutral proteinase (CANP), which is enriched in myelin, from brain. GM1, GD1a, GT1a, GM2, and GM4 produced a concentration‐dependent increase of mCANP activity. GD1a stimulated the greatest increase of enzyme activity (107%),
A K, Chakrabarti +3 more
openaire +2 more sources