Results 111 to 120 of about 735 (161)
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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 ...
Ken-Ichi Saito +2 more
exaly +3 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
Keiko Kamakura +2 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 ...
Masami Hayashi +2 more
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 +3 more sources
Journal of Biochemistry, 1983
The reaction of calcium activated neutral protease (CANP) with an epoxysuccinyl derivative (E64c) and iodoacetic acid (IAA) was examined in the presence of Ca2+, which specifically accelerates the rate of inactivation by these inhibitors. 1. E64c and IAA (100-fold molar excess) each inactivated CANP within a few minutes at 0 degrees C.
Koichi Suzuki, Suzuki Koichi
exaly +4 more sources
The reaction of calcium activated neutral protease (CANP) with an epoxysuccinyl derivative (E64c) and iodoacetic acid (IAA) was examined in the presence of Ca2+, which specifically accelerates the rate of inactivation by these inhibitors. 1. E64c and IAA (100-fold molar excess) each inactivated CANP within a few minutes at 0 degrees C.
Koichi Suzuki, Suzuki Koichi
exaly +4 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 Domańska-Janik +2 more
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 Domańska-Janik +2 more
exaly +3 more sources
FEBS Letters, 1983 The active site of calcium-activated neutral protease (CANP) was specifically labeled with iodoacetic acid. The active site hepta peptide was isolated from carboxymethylated CANP after digestion with proteases and the sequence was determined.
Koichi Suzuki +2 more
exaly +2 more sources
Calcium-activated neutral protease (CANP) in brain and other tissues
Progress in Neurobiology, 1984Un-Jin P Zimmerman, W W Schlaepfer
exaly +3 more sources
FEBS Letters, 1986 The complete amino acid sequence of the large subunit (catalytic subunit) of human low-Ca2+ requiring-calcium-activated neutral protease (μCANP) was deduced from its cDNA base sequence. It is composed of 714 amino acid residues and its sequence is highly
Shinobu Imajoh +2 more
exaly +2 more sources