Results 341 to 350 of about 191,378 (381)
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Apoptosis, 2006
Apoptosis can be mediated by different mechanisms. There is growing evidence that different proteolytic enzymes are involved in the regulation of apoptosis. Cathepsins are proteases which, under physiologic conditions, are localized intralysosomally.
C E, Chwieralski, T, Welte, F, Bühling
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Apoptosis can be mediated by different mechanisms. There is growing evidence that different proteolytic enzymes are involved in the regulation of apoptosis. Cathepsins are proteases which, under physiologic conditions, are localized intralysosomally.
C E, Chwieralski, T, Welte, F, Bühling
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Improved purification of cathepsin B1 and cathepsin B2
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975An improved purification of the cathepsins B1 and B2 from bovine spleen is described. In addition to the formerly used procedure, chromatography with DEAE-Sephadex or -cellulose and mercurated agarose is used. Both enzymes are obtained in an electrophoretically pure form but consist of two or more isoenzymes.
K, Otto, H, Riesenkönig
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Biochimica et Biophysica Acta (BBA) - General Subjects, 2003
Active cathepsin B has been found in cell extract and medium of human osteoblast-like cells and MG-63 cells. The released form is stable at neutral and alkaline pH and, in both cell types, intracellular and extracellular cathepsin B activities are increased by interleukin-1 beta (IL-1beta) and parathyroid hormone (PTH).
Aisa M. C. +3 more
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Active cathepsin B has been found in cell extract and medium of human osteoblast-like cells and MG-63 cells. The released form is stable at neutral and alkaline pH and, in both cell types, intracellular and extracellular cathepsin B activities are increased by interleukin-1 beta (IL-1beta) and parathyroid hormone (PTH).
Aisa M. C. +3 more
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Cathepsin L in glioma progression: Comparison with cathepsin B
Cancer Detection and Prevention, 2005Lysosomal cysteine cathepsins have been implicated in tumor progression. This study is aimed to reveal differential expression and compare the prognostic significance of cathepsins B and L in glioma patients.The histological slides of 82 patients with primary astrocytic tumors were reviewed.
Tadej, Strojnik +3 more
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CATHEPSIN B, CATHEPSIN C AND ARYLAMIDASE IN RABBIT CORNEA
Acta Ophthalmologica, 1982The 3 peptide hydrolases cathepsin B, cathepsin C and arylamidase have been assayed in rabbit cornea with the use of fluorigenic derivatives of β‐naphthylamine. The optimal reaction conditions and kinetic properties are described. The assay procedures which are simple and very sensitive can be used for studying the release of these enzymes from corneal
K, Schive, G, Volden
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Structural Differences Between Rabbit Cathepsin E and Cathepsin D
Biological Chemistry Hoppe-Seyler, 1986Rabbit cathepsins D and E were isolated from bone marrow. Both enzymes were purified by affinity chromatography on pepstatin-Sepharose 4B and Con A-Sepharose 4B. Purity of the enzymes was ascertained by two-dimensional gel electrophoresis after iodination. The isoelectric point of cathepsin D was found to be 6.95.
C, Lapresle +4 more
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1999
Aspartic proteinases are produced by a number of cells and tissues. These enzymes share a high degree of similarity which involves primary structures, and most of them are active predominantly in the acidic pH range. Eukaryotic aspartic proteinases (i.e.
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Aspartic proteinases are produced by a number of cells and tissues. These enzymes share a high degree of similarity which involves primary structures, and most of them are active predominantly in the acidic pH range. Eukaryotic aspartic proteinases (i.e.
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1977
Cathepsin D was purified from human liver by a procedure involving autolysis, acetone fractionation, and chromatography on ion-exchange media and organomercurial-sepharose. Multiple forms of the enzyme were then separated by preparative isoelectric focusing. The molecular weight of the protein was found to be 43,000.
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Cathepsin D was purified from human liver by a procedure involving autolysis, acetone fractionation, and chromatography on ion-exchange media and organomercurial-sepharose. Multiple forms of the enzyme were then separated by preparative isoelectric focusing. The molecular weight of the protein was found to be 43,000.
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Rat liver thiol proteinases: cathepsin B, cathepsin H and cathepsin L.
Acta biologica et medica Germanica, 1982Data on following points of lysosomal thiol proteinases (cathepsins B, H and L) from rat liver are described in this paper: Partial amino acid sequence of cathepsin B, substrate specificity of cathepsin L, immunological studies of cathepsin B and H and effectiveness of E-64, specific thiol proteinase inhibitor in vivo.
N, Katunuma +5 more
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