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Commission report on the present status of scientific knowledge and technical development regarding the use of sulphur dioxide for making wine; Proposal for a Council Regulation (EEC) amending Regulation (EEC) No 337/79 as regards maximum total sulphur dioxide levels in wines other than sparkling and liqueur wines (submitted by the Commission to the Council). COM (81) 730 final, 30 November 1981 [PDF]
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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 ...
K, Saito, R A, Nixon
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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
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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
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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
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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
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Hydrolysis of Protamine by Calcium-Activated Neutral Protease (CANP)
The 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
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Localization of calcium‐activated neutral protease (CANP) in the peripheral nerve
Muscle & 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
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Regulation of the calcium-activated neutral proteinase (CANP) of bovine brain by myelin lipids
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 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
A K, Chakrabarti +3 more
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Seventh Conference Real Time '91 on Computer Applications in Nuclear, Particle and Plasma Physics Conference Record, 2005
The author recals the earliest days of CAMAC development. He notes that in 5 years CAMAC was fully designed and had become a European and American Standard and was later recommended for world-wide use by the International Electrotechnical Commission.
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The author recals the earliest days of CAMAC development. He notes that in 5 years CAMAC was fully designed and had become a European and American Standard and was later recommended for world-wide use by the International Electrotechnical Commission.
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Primary structure and evolution of calcium-activated neutral protease (CANP)
Journal of Protein Chemistry, 1987The amino acid sequences of two subunits (80K and 30K) of calcium-activated neutral protease (CANP) were examined to clarify the structure-function relationship of CANP. The 80K subunit is composed of four clear domains (I–IV from the N-terminus). Domain II is a cysteine proteinase domain homologous to cathepsins B, L, and H.
K. Suzuki +4 more
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