Results 171 to 180 of about 20,637 (212)
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Current Medicinal Chemistry, 2006
Cathepsin B is an abundant and ubiquitously expressed cysteine peptidase of the papain family. It is involved in many physiological processes, such as remodeling of the extracellular matrix (wound healing), apoptosis, and activation of thyroxine and renin.
R, Frlan, S, Gobec
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Cathepsin B is an abundant and ubiquitously expressed cysteine peptidase of the papain family. It is involved in many physiological processes, such as remodeling of the extracellular matrix (wound healing), apoptosis, and activation of thyroxine and renin.
R, Frlan, S, Gobec
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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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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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Cathepsins Trigger Cell Death and Regulate Radioresistance in Glioblastoma
Cells, 2022Minghua Ren
exaly
[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, 2020Tom Houben +2 more
exaly