Results 191 to 200 of about 219,552 (223)
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Biochemistry, 1995
Glycyl endopeptidase is a cysteine endopeptidase of the papain family, characterized by specificity for cleavage C-terminal to glycyl residues only and by resistance to inhibition by members of the cystatin family of cysteine proteinase inhibitors. Glycyl endopeptidase has been crystallized from high salt with a substrate-like inhibitor covalently ...
O'Hara, Bernard P. +3 more
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Glycyl endopeptidase is a cysteine endopeptidase of the papain family, characterized by specificity for cleavage C-terminal to glycyl residues only and by resistance to inhibition by members of the cystatin family of cysteine proteinase inhibitors. Glycyl endopeptidase has been crystallized from high salt with a substrate-like inhibitor covalently ...
O'Hara, Bernard P. +3 more
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Chinese hamster ovary cells continuously secrete a cysteine endopeptidase
In Vitro Cellular & Developmental Biology, 1990The protease activity in serum-free conditioned medium of chinese hamster ovary (CHO) cells was measured using peptidyl (or aminoacyl)-4-methylcoumaryl-7-amides (MCAs) as the substrates. Aminopeptidase increased in level as amounts of nonviable cells increased during cultivation in serum-free medium, indicating that the activity seems to be originated ...
M, Satoh, S, Hosoi, S, Sato
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A high-molecular-weight cysteine endopeptidase from rat skeletal muscle
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983A cytosolic enzyme of high molecular weight (about 500 000), which attacks native or denatured proteins (inter alia, casein, globin and hexokinase) was purified about 1000-fold from mixed rat skeletal muscles, including muscles freed of mast cells by prior treatment of the animals with the degranulator, compound 48/80.
F, Ismail, W, Gevers
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Endogenous Action of Cysteine Endopeptidase and Three Carboxypeptidases on Triticale Prolamins
Cereal Chemistry, 2008ABSTRACTQuantitative and qualitative changes occurring in the prolamin fraction in the starchy endosperm of triticale grains were analyzed by SDS‐PAGE on consecutive days of germination. The most intensive hydrolysis of prolamins was observed after the second day of the process.
Adam Drzymała +3 more
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International Journal of Biological Macromolecules, 2019
Angiostrongylus cantonensis is a parasitic nematode dwelling in the heart and pulmonary arteries of rats, which can cause angiostrongyliasis in human by accidental infections, manifested as eosinophilic meningitis or meningoencephalitis.
Huifang Bai +6 more
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Angiostrongylus cantonensis is a parasitic nematode dwelling in the heart and pulmonary arteries of rats, which can cause angiostrongyliasis in human by accidental infections, manifested as eosinophilic meningitis or meningoencephalitis.
Huifang Bai +6 more
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A cysteine endopeptidase from barley malt which degrades hordein
Phytochemistry, 1989Abstract A cysteine endopeptidase of M r 29 000 which we have named malt endopeptidase-1 (MEP-1) was purified to homogeneity from a four-day green malt of barley ( Hordeum vulgare cv Schooner). It consists of two main species of pl 4.2 and 4.3 has a pH optimum of 4.5 for the hydrolysis of hordein and accounts for over a half of the hordein ...
Hilary A. Phillips, William Wallace
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Purification and partial characterization of a 31-kDa cysteine endopeptidase from germinated barley
Planta, 1996Proteolytic enzymes hydrolyze cereal seed storage proteins into small peptides and amino acids, which are very important for seed germination and the malting process. A cysteine-class endopeptidase was purified from 4-d-germinated barley (Hordeum vulgare L. cv. Morex).
N, Zhang, B L, Jones
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A RasMol study of the Mechanism of Inhibition of Cysteine Endopeptidase Enzyme Papain
Current Proteomics, 2009Cysteine endopeptidases regulate many physiological processes in the body and their impaired function may lead to several diseases. One of the methods of treating such diseases is achieved by controlling the proteolytic activity of these enzymes by using enzyme inhibition.
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1993
Cysteine endopeptidase inactivators were tested as inhibitors of interleukin 1-stimulated proteoglycan release from bovine nasal septum cartilage explants. Hydrophilic inactivators showed no inhibition at concentrations up to 100 microM. In contrast, lipophilic inactivators gave significant inhibition, which was both reversible and specific. No effects
D J, Buttle, J, Saklatvala, A J, Barrett
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Cysteine endopeptidase inactivators were tested as inhibitors of interleukin 1-stimulated proteoglycan release from bovine nasal septum cartilage explants. Hydrophilic inactivators showed no inhibition at concentrations up to 100 microM. In contrast, lipophilic inactivators gave significant inhibition, which was both reversible and specific. No effects
D J, Buttle, J, Saklatvala, A J, Barrett
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Biotechnology and applied biochemistry, 2015
S. Valdés‐Rodríguez +3 more
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S. Valdés‐Rodríguez +3 more
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