Results 251 to 260 of about 66,677 (282)
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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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Phospholipids activate cathepsin D
Biochemical and Biophysical Research Communications, 1983Total lipids as well as phospholipids extracted from the mitochondrial-lysosomal fraction of porcine adrenal cortex activated the lysosomal cathepsin D of this tissue 30- and 40-fold, respectively, with bovine serum albumin as the substrate. Phosphatidic acid, phosphatidyl ethanolamine, phosphatidyl serine, phosphatidyl inositol, phosphatidyl glycerol ...
S, Watabe, N, Yago
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Pleiotropic Effects of Cathepsin D
Endocrine, Metabolic & Immune Disorders - Drug Targets, 2009Over the past decades, the paradigm that lysosomal enzymes participate only in non-specific protein degradation during cell death has changed. Studies conducted both in cell cultures and in animals defined the role of these enzymes that includes cathepsin D (CD).
Aruna, Vashishta +2 more
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Cathepsin D: A cellular roadmap
Biochemical and Biophysical Research Communications, 2008Cathepsin D is a normal and major component of lysosomes, it is found in almost all cells and tissues of mammals. Present review describes different events in cellular life of cathepsin D mainly its biosynthesis, co-translational and posttranslational modifications, targeting to lysosomes and proteolytic processing and maturation within lysosomes.
Nousheen, Zaidi +3 more
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International Dairy Journal, 2000
Abstract Quarg cheese was produced from raw skim milk, pasteurised skim milk, raw skim milk with rennet added and ultrafiltrated raw skim milk. Quarg was also produced from raw skim milk with pepstatin added at curd cutting and from ultrafiltration retentate of raw milk with added pepstatin.
Hurley, M. J. +3 more
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Abstract Quarg cheese was produced from raw skim milk, pasteurised skim milk, raw skim milk with rennet added and ultrafiltrated raw skim milk. Quarg was also produced from raw skim milk with pepstatin added at curd cutting and from ultrafiltration retentate of raw milk with added pepstatin.
Hurley, M. J. +3 more
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Autolysis Studies of Cathepsin D
Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1982Incubation of the single polypeptide chain cathepsin D from bovine spleen at pH 3.5, resulted in the fragmentation of the molecule. This was followed by gel electrophoresis in the presence of dodecyl sulphate, gel filtration, circular dichroism and enzyme activity measurements.
T, Lah, V, Turk
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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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Breast Cancer Research and Treatment, 1990
Cathepsin D is an acidic lysosomal protease present in all cells. In estrogen receptor positive and negative breast cancer cell lines, the mRNA coding for pro-cathepsin D is overexpressed and sorting and maturation of the pro-enzyme are altered, leading to accumulation of the active proteinase in large endosomes and to secretion of the precursor (52K ...
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Cathepsin D is an acidic lysosomal protease present in all cells. In estrogen receptor positive and negative breast cancer cell lines, the mRNA coding for pro-cathepsin D is overexpressed and sorting and maturation of the pro-enzyme are altered, leading to accumulation of the active proteinase in large endosomes and to secretion of the precursor (52K ...
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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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