Results 201 to 210 of about 183,470 (243)
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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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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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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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Cysteine endopeptidase activity levels in normal human tissues, colorectal adenomas and carcinomas
International Journal of Cancer, 1991AbstractWe have assayed cysteine endopeptidase activities in 17 types of normal human tissue and in matched sets of colorectal mucosa, adenoma and carcinoma samples. Our data indicate that cathepsin B enzyme levels vary 70‐fold and cathepsin L enzyme levels vary 20‐fold from one normal tissue to another.
S, Shuja, K, Sheahan, M J, Murnane
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Biochemical characterization of a new cysteine endopeptidase from Carica candamarcensis L.
Plant Science, 1994Abstract This work describes a novel cysteine endopeptidase from C. candamarcensis L., which displays high esterase activity. The enzyme was isolated from latex collected from the unripe fruit and maintained at −20°C until processed. Purification was done by chromatography on Sephadex G-10, CM-Sephadex, SP-Sephadex, and thiol-Sepharose. The enzyme is
Marcelo Gravina de Moraes +2 more
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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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Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2007
The hard tick Rhipicephalus (Boophilus) microplus is a blood-sucking ectoparasite. R. microplus free-living stage comprises egg development, hatching, and subsequent larval development until encountering a host. In order to complete the embryological development, this tick relies on yolk reserve substances, mainly vitellin (Vt), which is still present ...
Andréia, Estrela +2 more
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The hard tick Rhipicephalus (Boophilus) microplus is a blood-sucking ectoparasite. R. microplus free-living stage comprises egg development, hatching, and subsequent larval development until encountering a host. In order to complete the embryological development, this tick relies on yolk reserve substances, mainly vitellin (Vt), which is still present ...
Andréia, Estrela +2 more
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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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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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Comparative Mass Spectrometric Analysis of Proteolytic Activity in Wine and Wine Vinegars.
Journal of Mass SpectrometryPlant-derived proteolytic enzymes are widely used in biochemistry and food processing. For example, bromelain, ficin, and papain serve as meat tenderizers, while cardosin A is used as a plant-based rennet in cheese production.
Michaela Rašková +2 more
semanticscholar +1 more source