Results 221 to 230 of about 20,584 (256)
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Cathepsin Activity in Cholesteatoma
Annals of Otology, Rhinology & Laryngology, 1985Collagenolytic cathepsin, presumed to play an important role in bone destruction of cholesteatoma, was investigated in cholesteatoma epithelium, subepithelial granulation tissue, skin from the bony external auditory meatus and, temporal bone. The enzyme extracted from tissues was proven to be lysosomal cathepsin B by SDS gel electrophoresis in the use ...
M, Iwanaga, E, Yamamoto, M, Fukumoto
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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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The action of cathepsin B and collagenolytic cathepsin in the degradation of collagen
1977Cathepsin B and collagenolytic cathepsin were obtained from bovine spleen and human placenta and identified as thiol proteinases. Both enzymes degraded insoluble fibrous collagen maximally at pH 3.5 and soluble monomeric collagen near pH 4.5. The response to activators and inhibitors was similar for both enzymes.
D J, Etherington, P J, Evans
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The Role of Cathepsins in Osteoimmunology
Critical Reviews in Eukaryotic Gene Expression, 2013Cathepsins are proteases comprising two small groups of serine and aspartic cathepsins and a large group of lysosomal cysteine cathepsins. Most of them are ubiquitously expressed throughout human tissues but some of them display a more restricted expression pattern and are involved in explicit tasks such as collagen degradation in the process of bone ...
Peter, Pietschmann +3 more
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Crystallization of cathepsin D
Biochemical and Biophysical Research Communications, 1976Summary Cathepsin D from chicken liver purified to apparent homogeneity by the method of affinity chromatography on pepstatin-Sepharose, was crystallized, upn gradual precipitation with ethanol, from 1.5% protein solution in slightly acid media corresponding to the isoelectric point of the enzyme.
O V, Kazakova, V N, Orekhovich
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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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[41] Cathepsin B, cathepsin H, and cathepsin L
1981Alan J. Barrett, Heidrun Kirschke
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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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The Ins and Outs of Cathepsins: Physiological Function and Role in Disease Management
Cells, 2020Tulasī Yadati +2 more
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