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  • 1
    Electronic Resource
    Electronic Resource
    Structural characterization of the N-glycans of a recombinant hepatitis B surface antigen derived from yeast (1992)
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 285-295 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00116a039
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  • 2
    Electronic Resource
    Electronic Resource
    Occurrence of 2-aminoethylphosphonic acid in human brain (1970)
    s.l. : American Chemical Society
    Biochemistry 9 (1970), S. 4866-4869 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00827a006
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  • 3
    Electronic Resource
    Electronic Resource
    Western blotting and isoform analysis of cathepsin D from normal and malignant human breast cell lines (1995)
    Springer
    Breast cancer research and treatment 35 (1995), S. 211-220 
    Details
    ISSN: 1573-7217
    Keywords: breast cancer ; cathepsin D isoforms ; Hs578Bst cells ; MCF7 cells ; MDA-MB-231 cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Cathepsin D from normal (Hs578Bst) and malignant (MCF7, MDA-MB-231) breast cell lines has been characterized with regard to its kinetic properties, activity levels, precursor and processed Mr forms, and isoform composition. Normal cell cathepsin D appears to have a more neutral pH optimum (pH 3.5) than the cancer cell line (pH 3.0–3.2) and greater activity between pH values of 4.0 to 4.5. The two cancer cell lines have approximately 1.5 to 2.0-fold increased total acid protease activity and 2 to 3-fold increased pepstatin-inhibitable protease activity (i.e. cathepsin D) when compared to the normal breast cell line. Western blotting indicates that a major processed form of cathepsin D for all three cell lines occurs at 31 kDa. The cancer cell lines contain significant amounts of cathepsin D precursors of 47 and 42 kDa whereas the normal cell line contains little if any of these precursors. Isoelectric focusing indicates that the normal cell line contains approximately 50% of its total acid protease activity at pIs above 4 whereas the cancer cell lines contain 70–80% of their protease activity at such pIs. In addition, the cancer cell lines contain two to three major isoforms between pIs of 5.5 and 6.3 which were not present in the normal cell line. The isoforms from pI values of 5.5 to 7.3 for all three cell lines are 100% pepstatin-inhibitable. In addition, Western blot analysis indicates that these isoforms contain the processed 31 kDa form of cathepsin D. The combined results indicate that the two breast cancer cell lines are similar to biopsied malignant breast tissue in exhibiting altered acid protease isoform profiles with increased relative amounts of pepstatin-inhibitable and immunoreactive acid protease activity (cathepsin D) compared to normal breast tissue or cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00668211
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  • 4
    Electronic Resource
    Electronic Resource
    Serum sialic acid and carcinoembryonic levels in the detection and monitoring of colorectal cancer (1990)
    Springer
    Diseases of the colon & rectum 33 (1990), S. 139-142 
    Details
    ISSN: 1530-0358
    Keywords: Sialic acid ; CEA ; Colorectal cancer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Total sialic acid (TSA), total protein (TP), TSA normalized to total TP (TSA/TP), and carcinoembryonic antigen levels were determined in 146 consecutive colorectal patients. These results were compared with results from 73 people with nonmalignant gastrointestinal disease, and with results from 96 normal controls. All malignancies were staged according to the Astler-Coller modification of Dukes' classification for colorectal cancer. All blood samples were drawn before surgical therapy. The TSA/TP ratio for colorectal cancer was 13.4 (mg/gm) in contrast to 12.1 (mg/gm) for pathologic controls, and 9.7 (mg/gm) for normal controls. Student's t test showed a P value less than 0.001 for normal controls and a P value less than 0.001 for pathologic controls. The TSA/TP also showed statistical significance in Dukes A, B2, C, and D subgroups when compared with normal controls. There were only four patients with stage Cl carcinoma, thus statistical analysis would be questionable. In contrast, carcinoembryonic antigen levels showed no significant elevations until Dukes C2 tumors were encountered. These preliminary findings suggest that TSA/TP ratio may detect colorectal cancer patients with less tumor burden and be more beneficial as a tumor marker than CEA for monitoring patients with colorectal cancer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02055544
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  • 5
    Electronic Resource
    Electronic Resource
    Analysis of cathepsin D in human breast cancer: Usefulness of the processsed 31 kDa active form of the enzyme as a prognostic indicator in node-negative and node-positive patients (2000)
    Springer
    Breast cancer research and treatment 60 (2000), S. 173-179 
    Details
    ISSN: 1573-7217
    Keywords: active processed cathepsin D ; breast cancer ; prognostic indicator ; survival analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The relative amounts of the precursor (52 kDa) and processed (31,27 kDa) forms of cathepsin D have been analyzed by Western blotting in biopsied breast tissue cytosols from 134 lesions from invasive breast cancer patients, 24 lesions from patients with ductal carcinoma in situ (DCIS), 227 lesions from benign breast disease patients, and 28 lesions from normal control subjects. The mean relative percentage amount of the 31 kDa form was significantly increased (p〈0.001) in the invasive breast cancer group compared to the other three groups. In addition, the mean relative percentage amount of the 31 kDa form was significantly increased (p〈0.05) in node-positive compared to node-negative breast cancer patients. In the benign breast disease group, patients with proliferative-type disease had a significantly increased (p=0.02) mean relative percentage amount of the 31 kDa form of cathepsin D compared to patients with nonproliferative-type disease. Invasive breast cancer patients were followed for up to 75 months to determine if the relative percentage amount of the 31 kDa form of cathepsin D was predictive of disease-free and overall survival. Although the amount of the 31 kDa form was not predictive of disease-free survival, patients in the ‘high’ 31 kDa group (〉18) were significantly (p〈0.05) more likely to die than patients in the ‘low’ 31 kDa group (≤18%). The 12 patients who died were all node-positive and in the high 31 kDa group. It thus appears that the relative amount of the processed, active 31 kDa form of cathepsin D is a useful prognostic indicator, at least in node-positive breast cancer patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006394401199
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  • 6
    Electronic Resource
    Electronic Resource
    Carbohydrate composition of purified human liver α-L-Fucosidase (1977)
    Springer
    Molecular and cellular biochemistry 18 (1977), S. 33-37 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Human liver α-L-fucosidase was purified to apparent homogeneity and analyzed for carbohydrate content primarily by gas-liquid chromatography (glc). The enzyme is about 7% carbohydrate by weight and contains the following sugars (residues per 50,000 molecular weight subunit): mannose (8.3), glucosamine (4.3) (presumably N-acetylated), sialic acid (1.6) and glucose (1.6). Galactose (0.8) and L-fucose (1.8) were also found but their presence may be due to artifacts of the purification procedure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00215277
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  • 7
    Electronic Resource
    Electronic Resource
    Isoenzymes of human liver α-L-fucosidase: Chemical relationship, kinetic studies, and immunochemical characterization (1978)
    Springer
    Molecular and cellular biochemistry 19 (1978), S. 171-180 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The chemical relationship of the seven forms of human liver α-L fucosidase has been studied by isoelectric focusing of neuraminidase- and sialyltransferase-treated preparations of α-L-fucosidase. Neuraminidase treatment leads to a decrease in the activity of the more acidic forms (IV–VII) and a concomitant increase in the activity of the more neutral forms (I–II). Incubation of the neuraminidase-treated fucosidase (forms I–III) with radiolabelled cytidine monophosphate-N-3H-acetylneuraminic acid and an enriched preparation of sialyltransferase devoid of fucosidase activity led to regeneration of the more acidic fucosidase isoenzymes (IV–VII) with the same isoelectric points and in nearly the same proportion as before neuraminidase treatment. These experiments suggest that the isoenzymes of human liver α-L-fucosidase are related, at least in part, by sialic acid residues. The seven isoenzymes of purified human liver α-L-fucosidase have been separated by preparative isoelectric focusing and characterized kinetically and immunochemically. Differences in Michaelis constants (Km's) and pH optimum curves were found for some of the isoenzymes. All seven isoenzymes were immunoprecipitated using the IgG fraction of anti-α-L-fucosidase antiserum suggesting that the presence of sialic acid residues does not affect the antigenicity of the forms of α-L-fucosidase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00225455
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  • 8
    Electronic Resource
    Electronic Resource
    Glycosphingolipid hydrolases: Properties and molecular genetics (1977)
    Springer
    Molecular and cellular biochemistry 17 (1977), S. 125-140 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary This is a review of the properties and molecular genetics of six lysosomal hydrolases:β-galactosidase, hexosaminidases A and B,α-galactosidase,β-glucosidase andα-fucosidase. Each enzyme is discussed with regards to isoenzymes and substrate specificity, subunit structure, genetic relationship of isoenzymes and genetic variants. The molecular genetics of human diseases caused by deficiencies of each enzyme are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01730832
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  • 9
    Electronic Resource
    Electronic Resource
    Purification and Characterization of Cathepsin D from Normal Human Breast Tissue (1997)
    Springer
    The protein journal 16 (1997), S. 171-181 
    Details
    ISSN: 1573-4943
    Keywords: Cathepsin D ; human breast ; aspartyl protease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The lysosomal aspartyl protease cathepsin D is present in most mammalian cells and is active in the catabolism of intracellular and endocytosed proteins. It appears to be overexpressed and abnormally secreted in breast cancer cells, and may contribute to the process of tumor metastasis. In the present study, cathepsin D was purified 4500-fold from normal human breast tissue using pepstatin-agarose, DEAE Sephadex, and Sephadex G-75 chromatography. The resulting enzyme on SDS-PAGE contained five protein bands (47, 31, 29, 13, and 12kDa) which were all immunoreactive on western blot analysis using anti-cathepsin D polyclonal antibodies. The isoform profile of purified cathepsin D consisted of three major peaks at approximate pI 7.3, 6.8, and 6.3, and a broad area of lower activity between pI of 5.0 and 2.0. The purified enzyme had a broad pH optimum centered around pH 3.3. Lectin blotting indicated that cathepsin D is a glycoprotein which is recognized by Galanthus nivalis agglutinin and concanavalin A, suggesting the presence of mannose residues. However, Sambucus nigra agglutinin, Tetragonolobus purpureas agglutinin, Triticum vulgaris agglutinin, and Erythrina cristagalli agglutinin failed to recognize cathepsin D, suggesting a lack of lectin-available sialic acid, fucose, N-acetylglucosamine, and galactose residues, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026322707644
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  • 10
    Electronic Resource
    Electronic Resource
    The effect of alkaline borohydride treatment onN-linked carbohydrates of glycoproteins (1989)
    Springer
    Glycoconjugate journal 6 (1989), S. 45-56 
    Details
    ISSN: 1573-4986
    Keywords: ribonuclease-B ; glyco-asparagines ; oligosaccharide-alditols ; 1 H-NMR spectroscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The effects of treatments of the glycoprotein ribonuclease-B, the proteins ribonuclease-A and myoglobin, and the glyco-amino acid GlcNAcβ(1-N) Asn with alkalil alkaline sodium borohydride, and aqueous sodium borohydride were systematically studied as a function of the concentration of the reagents, the temperature, and the length of the treatment. High-field1H-NMR spectroscopy, chromatographic methods and amino-acid analysis were used to characterize products of the treatments of the various compounds. Our results indicate that mild alkaline borohydride treatment, as well as aqueous borohydride treatment alone, is capable of extensively degrading polypeptides and of partially releasing theN-linked glycans from ribonuclease-B. Initially, glycopeptides are produced, the peptide portion of which consists of several amino acids, which are further hydrolyzed to yield a mixture of glyco-asparagines and oligosaccharide-alditols in the ratio of ≈4:1. Strong alkaline borohydride treatment of ribonuclease-B is capable of completely releasing theN-linked carbohydrates as oligosaccharide-alditols.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01047889
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