Results 291 to 300 of about 25,778,187 (334)
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The action of cathepsin B and collagenolytic cathepsin in the degradation of collagen

1977
Cathepsin 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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IMMUNOHISTOCHEMICAL STUDY ON CATHEPSIN-B AND CATHEPSIN-D IN PANCREATIC-CANCER

Oncology Reports, 1994
Lysosomal enzymes, cathepsin B and D, have been studied in their possible relationship to the ability of malignant cells to invade and metastasize. In the current investigation, these cathepsins were detected immunohistochemically using avidin-biotin-peroxidase complex method in the pancreatic cancer cells of 21 patients.
B, Nakata   +8 more
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Intracellular distribution of cathepsin B and cathepsin C in rat liver

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
Summary 1. The intracellular distribution of cathepsin B and cathepsin C (EC 3,4,4.9) in rat liver has been investigated by means of differential and density-equilibrium centrifugation, activation and solubilization experiments. 2. The enzymes appear to be localized in the lysosomes.
J M, Bouma, M, Gruber
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Death by Cathepsin B

Science Signaling, 2001
Apoptosis (programmed cell death) is defined by specific biochemical and morphological markers that include chromatin condensation and fragmentation. Evidence is mounting that pathways involving cathepsins may be important for apoptotic cell death. Foghsgaard et al.
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Purification and properties of rabbit liver cathepsin M and cathepsin B

Archives of Biochemistry and Biophysics, 1985
Cathepsins M and B from rabbit liver lysosomes were separated by chromatography on Ultrogel AcA34 at low ionic strength and purified to homogeneity, and their catalytic and molecular properties were compared. Cathepsin M was relatively inactive with synthetic peptide substrates.
Erickson Viitanen S   +5 more
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Serum cathepsin B levels, urinary excretion of cathepsin B and tissue cathepsin B content in the patients with gastric cancer.

Nihon geka hokan. Archiv fur japanische Chirurgie, 1994
Serum cathepsin B levels and urinary excretion of cathepsin B in the patients with gastric cancer were significantly higher than those in the control non-cancer patients. Moreover, cancer tissue cathepsin B content was significantly higher than that in the normal tissue.
T, Hirano, H, Yoshioka
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The specificity of cathepsin B.

Acta biologica et medica Germanica, 1982
Peptidyl chloromethyl ketones, largely derived from arginine, inactivate cathepsin B (beef spleen) at rates that vary 300 fold according to sequence, but the residue in the P1 position is not responsible for this variation since homoarginine or nitroarginine in this position provide inhibitors as good or better than those containing arginine.
E, Shaw, C, Kettner
openaire   +1 more source

Cathepsin B links oxidative stress to the activation of NLRP3 inflammasome

Experimental Cell Research, 2018
H. Bai   +5 more
semanticscholar   +1 more source

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