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  • 1
    Electronic Resource
    Electronic Resource
    Purification and Chemical Characterization of β-Trace Protein from Human Cerebrospinal Fluid: Its Identification as Prostaglandin D Synthase (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 61 (1993), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: β-Trace protein from pooled human CSF was purified to homogeneity. An apparent molecular mass of 23–29 kDa was determined for the polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amino-terminal sequencing of the polypeptide yielded the unique amino acid sequence APEAQVSVQPNFQQDKFLGRWFSA24. Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of β-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9α, 11 a-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2]. A conservative amino acid exchange (The instead of Ser) was detected at amino acid position 154 of the β-trace polypeptide chain in the corresponding tryptic peptide. The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate. Carbohydrate compositional as well as methylation analysis indicated that Asn29and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with α2–3- and/or α2–6-linked N-acetylneuraminic acid) that are almost quantitatively α1-6 fucosylated at the proximal N-acetylglucosamine; ∼70% of these molecules contain a bisecting N-acetylglucosamine. Agalacto structures as well as those with a peripheral fucose are also present.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1993.tb02145.x
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  • 2
    Electronic Resource
    Electronic Resource
    Carbohydrate Structures of β-Trace Protein from Human Cerebrospinal Fluid: Evidence for “Brain-Type”N-Glycosylation (1994)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 63 (1994), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The carbohydrate structures of β-trace protein from human cerebrospinal fluid have been elucidated. This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56). Enzymatically released N-glycans were studied by compositional and methylation analyses, high-pH anion-exchange chromatography, and liquid secondary ion mass spectrometry. All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues. The rest were triantennary chains or biantennary chains with intact or truncated lactosamine repeats. The innermost N-acetylglucosamine residues of nearly all structures were found to be α1,6-fucosylated. Peripheral fucose (about 20%α1,3-linked to N-acetylglucosamine) was also detected. Seventy percent of the oligosaccharides contained a bisecting N-acetylglucosamine. Especially in the neutral, but also in the monosialylated oligosaccharide fractions, many incomplete antennae consisting of N-acetylglucosamine only were present. At least 20 different N-glycans were identified. Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences. According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in α2,3 linkage), this protein can be classified as “brain-type” glycosylated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1994.63062185.x
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  • 3
    Electronic Resource
    Electronic Resource
    Protein Composition, IgG, and IgA Analysis in the Saliva of Patients with Multiple Sclerosis (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 694 (1993), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1993.tb18372.x
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  • 4
    Electronic Resource
    Electronic Resource
    Isoenzyme der Lactatdehydrogenase im Glaskörper des Rindes (1974)
    Springer
    Graefe's archive for clinical and experimental ophthalmology 189 (1974), S. 309-321 
    Details
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Im Glaskörper und den angrenzenden Geweben des Rinderauges wurden die Enzymaktivitäten von LDH, MDH, GOT, PGI und CHE gemessen. Auftrennung der LDH-Isoenzyme des Glaskörpers mit der Agargelelektrophorese ergab für Bande 1: 65,4%, 2: 14,3, 3: 7,5, 4: 6,4 und Bande 5: 6,3%. Obwohl Glaskörper damit ein Herz-Typ-Muster aufweist, sind Rückschlüsse auf eine oxidative Stoffwechsellage nicht berechtigt. Vielmehr ist Glaskörper den in ihren metabolischen Fähigkeiten stark reduzierten Erythrocyten, Thrombocyten und Linsenfasern zuzurechnen, die mit einer H-Typ LDH glykolysieren. Aufgrund der guten Übereinstimmung zwischen Glaskörper und Hyalocyten im (Iso-)Enzymmuster werden die Glaskörperrindenzellen als Herkunftsort der Enzyme im Glaskörper postuliert.
    Notes: Summary The activities of LDH, MDH, GOT, PGI and CHE have been determined in the vitreous body and adjacent tissues of cattle-eye. LDH-Isoenzymes were separated with agar gel electrophoresis. Isoenzyme 1 of vitreous accounts for 65.4%, 2 for 14.3, 3 for 7.5, 4 for 6.4, 5 for 6.3%. Though this clearly demonstrates a heart-type pattern, an oxidative metabolism should not be concluded. Vitreous body rather belongs to the metabolically restricted erythrocytes, platelets and lens-fibers which depend on anaerobic glycolysis despite an aerobic LDH pattern. Since there is good agreement between the (iso-)enzyme ratios of vitreous body and hyalocytes, the cortex cells are thought to represent the origin of vitreous enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02384857
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  • 5
    Electronic Resource
    Electronic Resource
    Differentiation of proteinurias with electrophoresis (1991)
    Springer
    Pediatric nephrology 5 (1991), S. 376-378 
    Details
    ISSN: 1432-198X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01453655
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  • 6
    Electronic Resource
    Electronic Resource
    Bedeutung und Herkunft der Enzyme im Glaskörper des Rindes (1974)
    Springer
    Graefe's archive for clinical and experimental ophthalmology 190 (1974), S. 79-96 
    Details
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Im Glaskörper des Rindes wurden sämtliche Enzyme der Glykolyse, Malatdehydrogenase, die Transaminasen GOT und GPT sowie alkal. Phosphatase nachgewiesen. Die Enzymmuster des Glaskörpers und seiner Zellen entsprechen einander, während die Verteilung im Serum deutlich abweicht, weshalb die Hyalocyten als hauptsächlicher Ursprungsort für die enzymatisch aktiven löslichen Proteine des Glaskörpers angenommen werden. Die Ähnlichkeit des Enzymmusters mit anderen Bindegeweben unterstreicht die mesenchymale Natur des Glaskörpers. Wie alle bisher untersuchten Gewebearten weist auch Glaskörper konstante Proportionen der Enzyme der „Phospho-Triose-Glycerat-Gruppe“ auf. Die Aktivität der extracellulären Enzyme könnte ausreichen, um den minimalen Stoffwechsel des Glaskörpers zu bewerkstelligen.
    Notes: Summary The presence of malatedehydrogenase, alkal. phosphatase, GOT- and GPT-aminotransferases and of all glycolytic enzymes in the vitreous body of cattle was demonstrated. As the enzyme patterns of vitreous body and its cells show remarkable similarity, the serum pattern differing significantly, the cortex cells presumably represent the origin of the enzymatically active soluble proteins in the vitreous. Enzyme distribution in vitreous shows the same features as in other connective tissues thus indicating its mesenchymal nature. The “phospho-triose-glycerate-group” of enzymes has been found in the same constant proportions as in other tissues. The activities of its extracellular enzymes could be sufficient to account for the minimal metabolic requirements of the vitreous.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414338
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