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Reflections on a long career in Neuropathology. [PDF]
Free NeuropatholFarrell M.
europepmc +1 more source
人血小板Ca2+依存性中性プロテアーゼ（CANP）-その内因性基質と低Ca2+要求性CANP（μ-CANP）の精製
人血小板Ca2+依存性中性プロテアーゼ（CANP）-その内因性基質と低Ca2+要求性CANP（μ-CANP）の精製openaire
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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, Nixon Ralph A
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
S Ishiura, Hideo Sugita
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 ...
Kazutomo Imahori +2 more
exaly +3 more sources
Calcium-activated neutral protease (CANP) in brain and other tissues
Progress in Neurobiology, 1984William W Schlaepfer +2 more
exaly +3 more sources