Results 251 to 260 of about 113,729 (277)
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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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Specificity of Rat Liver Cathepsin D
Journal of Biochemistry, 1987The specificity of highly purified rat liver cathepsin D was investigated by analyzing the digests of denatured proteins. At the P1 site, cathepsin D prefers hydrophobic residues except Ile and Val, that are branched at the beta-carbon. Strong and weak hydrophobicities are required at P1' and P2 sites, respectively.
T, Imoto, K, Okazaki, H, Koga, H, Yamada
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Cathepsin D activity in nasal polyps
Clinical Biochemistry, 2012The aim of the study was to assess the activity of cathepsin D in polyps removed during first-time FESS surgery and in recurrent polyps removed during successive FESS surgeries.The study examined 24 polyps: 11 polyps were removed during first-time surgical procedures (termed primary polyps in the study), and 13 recurrent polyps were removed in ...
Katarzyna, Pawłowska-Góral +4 more
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Cathepsin D Content in Colorectal Cancer
Oncology, 1995Cathepsin D content and activity were determined in matched paired sets of colorectal tumor tissue and normal mucosa and correlated with a number of biological and clinical parameters. Significantly higher cathepsin D activity was measured in tumor cytosol compared to paired normal mucosa (p < 0.02), in Dukes’ stage A tumors compared to Dukes’ B and
Tumminello F. M. +5 more
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Proteolysis of IGFBPs by cathepsin D in vitro and in cathepsin D-deficient mice
Progress in Growth Factor Research, 1995Affinity-purified lysosomal protease cathepsin D cleaved recombinant human IGFBP-1 to -5 in fragments of defined sizes, while IGFBP-6 was not degraded. To assess the role of cathepsin D for proteolytic processing of IGFBP in vivo, serum from cathepsin D-deficient mice and conditioned media from cathepsin D-deficient fibroblasts and organ explants were ...
T, Braulke +8 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.
openaire +1 more source