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  • 1
    Electronic Resource
    Electronic Resource
    Sonderfälle von Vergiftungsmöglichkeiten durch Arsenwasserstoff (1932)
    Springer
    International archives of occupational and environmental health 3 (1932), S. 496-508 
    Details
    ISSN: 1432-1246
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02125114
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  • 2
    Electronic Resource
    Electronic Resource
    Untersuchungen über Wandisolationen unter sommerlichen Verhältnissen (1923)
    Springer
    Medical microbiology and immunology 99 (1923), S. 359-365 
    Details
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02284710
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  • 3
    Electronic Resource
    Electronic Resource
    Der Zinkstaub im gewerblichen Betriebe, seine Einwirkung auf den Gesundheitszustand der Arbeiter und seine Ablagerung in den Organen (1929)
    Springer
    Medical microbiology and immunology 109 (1929), S. 598-610 
    Details
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02175779
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  • 4
    Electronic Resource
    Electronic Resource
    Untersuchungen über die Wärmeökonomie isolierter und nichtisolierter Siedlungsbauten in hygienischer und wirtschaftlicher Beziehung (1925)
    Springer
    Medical microbiology and immunology 105 (1925), S. 113-137 
    Details
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02175085
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  • 5
    Electronic Resource
    Electronic Resource
    Inability of the human fecal microflora to metabolize the nonabsorbable fat substitute, olestra (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 328-334 
    Details
    ISSN: 1476-5535
    Keywords: GI microflora ; Bacterial catabolism ; Fat substitute ; Olestra
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Olestra is a non-caloric fat substitute under review by the Food and Drug Administration. It consists of a mixture of octa-, hepta- and hexaesters of sucrose formed with long chain fatty acids. Previous studies showed olestra is not hydrolyzed by mammalian lipases and is not absorbed. The objective of this study was to evaluate the potential for colonic microflora to metabolize olestra after continued exposure. Neat and emulsified14C-[fatty acid] olestra was incubated for 72 h in both minimal and organically-enriched anaerobic media inoculated with feces from seven subjects who had consumed olestra (9 g per day) over a 3–4 week period.14C-sucrose and14C-glucose served as positive controls. Production of14CO2,14CH4,14C-volatile fatty acids (VFAs) and14C-long chain fatty acids (LCFAs) was determined. In addition, the ester distribution and fatty acid composition of olestra were examined before and after incubation. Significant quantities of14CO2 and14C-VFAs were generated from the14C-sugars, indicating that the microflora were active under the incubation conditions. Furthermore, free oleic acid was extensively hydroxylated and hydrogenated. In contrast, no degradation products (gas, VFAs, LCFAs) or changes in the olestra resulting from bacterial activity were detected. These results indicate that under anaerobic conditions the colonic microflora of the humans, consuming olestra, did not metabolize olestra.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01569736
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  • 6
    Electronic Resource
    Electronic Resource
    Isolation and Characterization of Two Forms of an Acidic Bromelain Stem Proteinase (1998)
    Springer
    The protein journal 17 (1998), S. 351-361 
    Details
    ISSN: 1573-4943
    Keywords: Bromelain ; cysteine proteinase ; FPLC ; amino acid sequence analysis ; mass spectroscopy ; monosaccharide analysis ; kinetic parameters
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Two forms of an acidic bromelain proteinase isolated from crude bromelain, an extract from pineapple stem, were found by a two-step FPLC purification procedure. The basic main components were removed by cation exchange chromatography and the breakthrough fraction was further resolved by anion exchange chromatography into 15 protein fractions, only two of which, called SBA/a and SBA/b, were proteolytically active. These components were characterized by electrospray mass spectroscopy (ESMS), isoelectric focusing, N-terminal amino acid sequence analysis, monosaccharide analysis, and enzymatic parameters. The molecular masses of SBA/a and SBA/b were determined by ESMS to be 23,550 and 23,560, respectively. The isoelectric points (pI) of the two bands of SBA/a were 4.8 and 4.9; SBA/b focused as a single band at pI = 4.8. Partial N-terminal amino acid sequences (11 residues) were identical to SBA/a and SBA/b and identical with those of stem bromelain, the basic main proteinase of the pineapple stem, and fruit bromelain, the acidic main proteinase of the pineapple fruit. Both components are highly glycosylated; hydrolysis of SBA/a yielded about twofold more monosaccharide per protein than SBA/b. The comparison of the catalytic properties of SBA/a with those of SBA/b revealed no relevant differences in the hydrolysis of three peptidyl-NH-Mec substrates and in the inhibition profiles using chicken cystatin and E-64, indicating that these components can be considered as two forms of a single enzyme. Both forms are scarcely inhibited by chicken cystatin and slowly inactivated by E-64, hence are nontypical cysteine proteinases of the papain superfamily.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1022507316434
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  • 7
    Electronic Resource
    Electronic Resource
    Isolation and partial characterization of basic proteinases from stem bromelain (1995)
    Springer
    The protein journal 14 (1995), S. 41-52 
    Details
    ISSN: 1573-4943
    Keywords: Bromelain ; basic proteinases ; amino acid sequence analysis ; FPLC ; mass spectroscopy ; monosaccharide composition analysis ; pH optimum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Crude bromelain extracts from pineapple stems (Ananas comosus) were fractionated by two-step FPLC-cation-exchange chromatography. At least eight basic proteolytically active components were detected. The two main components F4 and F5 together with the most active proteinase fraction F9 were characterized by SDS-PAGE, mass spectroscopy, multizonal cathodal electrophoresis, partial amino acid sequence, and monosaccharide composition analysis. F9 amounts to about 2% of the total protein and has a 15 times higher specific activity against the substratel-pyroglutamyl-l-phenylanalyl-l-leucine-p-nitroanilide (PFLNA) than the main component F4. The molecular masses of F4, F5, and F9 were determined to 24,397, 24,472, and 23,427, respectively, by mass spectroscopy. Partial N-terminal amino acid sequence analysis (20 amino acids) revealed that F9 differs from the determined sequence of F4 and F5 by an exchange at position 10 (tyrosine→serine) and position 20 (asparagine→ glycine). F4 and F5 contained fucose, N-acetylglucosamine, xylose, and mannose in ratio of 1.0∶2.0∶1.0∶2.0, but only 50% of the proteins seem to be glycosylated, whereas F9 was found to be unglycosylated. Polyclonal antibodies (IgG) against F9 detected F4 and F5 with tenfold reduced reactivity. ThepH optimum of F4 and F5 was betweenpH4.0 and 4.5 and for F9 close to neutralpH. The kinetic parameters for PFLNA hydrolysis were similar for F4 (K m 2.30 mM,k cat 0.87 sec−1 and F5 (K m 2.42 mM,k cat 0.68 sec−1), and differed greatly from F9 (K m 0.40 mM,k cat 3.94 sec−1).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01902843
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  • 8
    Electronic Resource
    Electronic Resource
    Praktische Erfahrungen über das Verhalten von Kleinhäusern aus “Ersatzbaustoffen” (1923)
    Springer
    Medical microbiology and immunology 99 (1923), S. 350-358 
    Details
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02284709
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  • 9
    Electronic Resource
    Electronic Resource
    N-Glycosylation of membrane glycoproteins in retinol-deficient rat liver (1992)
    Springer
    Glycoconjugate journal 9 (1992), S. 132-140 
    Details
    ISSN: 1573-4986
    Keywords: Vitamin A ; retinol ; N-linked oligosaccharides ; membrane glycoproteins ; dipeptidylpeptidase IV
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The effect of vitamin A deficiency onN-linked oligosaccharides of membrane glycoproteins was studied in rat liver in order to evaluate the suggested role of retinol in proteinN-glycosylation. First, oligosaccharides of newly synthesized glycoproteins from rough endoplasmic reticulum of vitamin A deficient liver were compared with that of pair-fed controls. Oligosaccharides were metabolically labelled withd-[2-3H]mannose, released from the glycoproteins with endoglycosidase H, purified by reversed phase HPLC and ion exchange chromatography, and were reduced with sodium borohydride. HPLC fractionation of the oligosaccharide alditols showed that the glycoproteins carried mainly four oligosaccharide species, Glc1Man9GlcNAc2, Man9GlcNAc2, Man8GlcNAc2 and Man7GlcNAc2, in identical relative amounts in the vitamin A deficient and the control tissue. In particular, no increase in the proportion of short chain oligosaccharides was noted in vitamin A deficient liver. Second, the number ofN-linked oligosaccharides was estimated in dipeptidylpeptidase IV (DPP IV), a major glycoprotein constituent of the hepatic plasma membrane, comparing the newly synthesized glycoprotein from rough endoplasmic reticulum and the mature form of DPP IV from the plasma membrane. No evidence was obtained that retinol deficiency caused incomplete glycosylation of this membrane glycoprotein. From these data, the suggested role of retinol as a cofactor involved in the synthesis ofN-linked oligosaccharides of glycoproteins must be questioned.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00780760
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  • 10
    Electronic Resource
    Electronic Resource
    Optimized deglycosylation of glycoproteins by peptide-N4-(N-acetyl-β-glucosaminyl)-asparagine amidase fromFlavobacterium meningosepticum (1990)
    Springer
    Glycoconjugate journal 7 (1990), S. 279-286 
    Details
    ISSN: 1573-4986
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F (PNGase F) fromFlavobacterium meningosepticum is a highly useful enzyme for the structural analysis of N(asparagine)-linked carbohydrate chains derived from glycoproteins. The enzyme was enriched using a published procedure [Tarentino AL, Gomez CM, Plummer TH, Jr (1984) Biochemistry 1985:4665–71; Tarentino AL, Plummer TH, Jr (1987) Methods Enzymol 138:770–78] and further purified by hydrophobic interaction HPLC on a weak hydrophobic TSK-Ether column from which it was eluted by a decreasing gradient of 1.7 M ammonium sulphate in 100 mM sodium phosphate, pH 7.0, containing 5 mM EDTA. To determine the optimal conditions for a complete deglycosylation of glycoproteins by PNGase F, experiments were performed with humanα 1-acid glycoprotein, because the five complex type carbohydrate chains are quite resistant to enzymic hydrolysis. The influence of different detergents on the enzyme reaction was studied. Complete deglycosylation of humanα 1-acid glycoprotein was achieved by the use of 60 mU/ml PNGase F in 0.25 M sodium phosphate buffer, pH 8.6, containing 0.2% (w/v) SDS, 20 mM mercaptoethanol and 0.5% Mega-10.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01073372
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