Results 121 to 130 of about 277 (144)
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Cysteine Endopeptidases and Their Inhibitors in Malignant Progression of Rat Embryo Fibroblasts
Biological Chemistry Hoppe-Seyler, 1992Cathepsins B and L and their endogenous inhibitors were evaluated in rat embryo fibroblast lines which have been developed as a model system for the study of malignant progression and metastatic capability. Three groups of lines were analyzed: 1) immortalized/non-tumorigenic, 2) tumorigenic/metastatic lines transfected with c-Ha-ras, and 3) metastatic ...
Grace Ziegler +5 more
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Decrease in vivo of cysteine endopeptidases in blood of patients with tumor of the larynx
Anti-Cancer Drugs, 1993Since cysteine endopeptidase (cathepsins B and L) have been proposed to be implicated in tumor malignancy, we have attempted to decrease these in vivo. Large amounts of urine cysteine peptidase inhibitors (UCPI) are present in the urine of patients.
Berdowska I +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.
Firhaad Ismail, Wieland 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 ...
H.A. Phillips, William Wallace
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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.
Wiesław Bielawski +3 more
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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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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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[36] Cysteine endopeptidases of parasitic protozoa
1994Publisher Summary This chapter describes techniques that are generally applicable in studies of protozoan cysteine endopeptidases. Sample preparation varies from parasite to parasite, but in general cells are lysed in detergent-containing solutions, although repeated freezing and thawing can also be used to release cysteine endopeptidases.
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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.
Kieran Sheahan +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).
Ningyan Zhang, Berne I. Jones
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