Results 131 to 140 of about 735 (161)

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
openaire   +2 more sources

[Polymorphism of exon 4 in the CANP-3 gene in patients with primary myopathies].

Genetika, 2000
The structures of the gene for calpain (CANP-3) and of the DMD gene were analyzed in patients with primary myopathies [limb-girdle muscular distrophy (LGMD) and Duchenne-Becker myodystrophy (DBM)] from various regions of Russia. Via amplification of DNA isolated from the peripheral blood lymphocytes of 74 patients, extended deletions were found in 18 ...
N A, Lipatova, I N, Krakhmaleva, S S, Shishkin, N I, Shakhovskaia, N I, Podnikova, I N, Lunga, M A, Tarksh, N L, Gerasimova   +7 more
openaire   +1 more source

The regional and subcellular distribution of calcium activated neutral proteinase (CANP) in the bovine central nervous system

Neurochemical Research, 1989
Calcium-activated neutral proteinase (CANP) activity was determined in subcellular fractions and in different regions of bovine brain. The CANP specific activity in spinal cord and corpus callosum, areas rich in myelin, were almost six-fold greater than cerebral cortex and cerebellum.
A K, Chakrabarti, N L, Banik, J M, Powers, E L, Hogan   +3 more
openaire   +2 more sources

Structure and function of the small (30K) subunit of calcium-activated neutral protease (CANP).

Biomedica biochimica acta, 1987
Calcium-activated neutral protease (CANP), a typical intracellular protease, is composed of a catalytic 80K subunit (80K) and a 30K subunit (30K) of unknown function. The structure of rabbit CANP 30K was examined to clarify its role in the enzyme function. It has a clear two-domain structure composed of 266 amino acid residues.
K, Suzuki, Y, Emori, S, Ohno, S, Imahori, H, Kawasaki, S, Miyake   +5 more
openaire   +1 more source

Effect of metal ions on the structure and activity of calcium-activated neutral protease (CANP).

Journal of biochemistry, 1983
To clarify the mechanism of activation of calcium activated neutral protease (CANP, or mCANP: active at mM Ca2+), the structure of mCANP was examined by measuring CD spectra and by titration of SH groups in the presence of Mn2+. Mn2+ significantly increases the sensitivity of CANP to Ca2+ but CANP is not active with Mn2+ alone.
K, Suzuki, S, Ishiura
openaire   +1 more source

I think I canp I think I canp Reconsidering the place for practice methodologies in psychological research.

Professional Psychology: Research and Practice, 1993
openaire   +1 more source

Modulation of Ca++-activated neutral protease /CANP/ activity by propranolol in rat heart

Journal of Molecular and Cellular Cardiology, 1987
T ZALEWSKA, B KWIATKOWSKAPATZER
openaire   +1 more source

Control mechanism of calcium-activated neutral protease (CANP) activity

1986
G. Kawashima, M. Inomata, K. Imahori
openaire   +1 more source

Profile: James C. McCann, Jr., RN, DNSc, CANP

Journal of Psychosocial Nursing and Mental Health Services, 2001
openaire   +1 more source

The Amino-Terminal Hydrophobic Region of the Small Subunit of Calcium-Activated Neutral Protease (CANP) Is Essential for Its Activation by Phosphatidylinositol1

Journal of Biochemistry, 1986
Shinobu Imajoh, Hiroshi Kawasaki, Koichi Suzuki   +2 more
exaly