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  • Cell & Developmental Biology  (3)
  • Coleus (cell cultures)  (2)
  • Animals
  • METEOROLOGY AND CLIMATOLOGY
  • 1990-1994  (6)
  • 1
    Electronic Resource
    Electronic Resource
    Purification of rosmarinic acid synthase from cell cultures of Coleus blumei Benth (1993)
    Springer
    Planta 191 (1993), S. 18-22 
    Details
    ISSN: 1432-2048
    Keywords: Coleus (cell cultures) ; Hydroxycinnamic acid ester ; Rosmarinic acid ; Rosmarinic acid synthase (purification)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rosmarinic acid synthase from cell cultures of Coleus blumei Benth. was purified to apparent homogeneity by fractionated ammonium sulfate precipitation (60–80% saturation), hydrophobic interaction chromatography, affinity chromatography and gel filtration. This purification procedure resulted in a 225-fold-enriched specific enzyme activity with a yield of 9%. The protein preparation was apparently pure according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimensional gel electrophoresis. The apparent molecular mass determined by gel filtration and SDS-PAGE was 77 kDa, indicating that rosmarinic acid synthase is a monomeric enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00240891
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  • 2
    Electronic Resource
    Electronic Resource
    Proposed biosynthetic pathway for rosmarinic acid in cell cultures of Coleus blumei Benth (1993)
    Springer
    Planta 189 (1993), S. 10-14 
    Details
    ISSN: 1432-2048
    Keywords: Coleus (cell cultures) ; Hydroxycinnamic acid ester ; Phenylpropanoid metabolism ; Rosmarinic acid (biosynthetic pathway)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A biosynthetic pathway for rosmarinic acid is proposed. This pathway is deduced from studies of the enzymes detectable in preparations from suspension cells of Coleus blumei. Phenylalanine is transformed to 4-coumaroyl-CoA by the enzymes of the general phenylpropanoid pathway: phenylalanine ammonia-lyase (EC 4.3.1.5), cinnamic acid 4-hydroxylase (EC 1.14.13.11) and hydroxycinnamic acid:CoA ligase (EC 6.2.1.12). Tyrosine is metabolized to 4-hydroxyphenyllactate by tyrosine aminotransferase (EC 2.6.1.5) and hydroxyphenylpyruvate reductase. The ester can be formed from 4-coumaroyl-CoA and 4-hydroxyphenyllactate by the catalytic activity of rosmarinic acid synthase with concomitant release of CoA. Microsomal hydroxylase activities introduce the hydroxyl groups at positions 3 and 3′ of the aromatic rings of the ester 4-coumaroyl-4′-hydroxyphenyllactate giving rise to rosmarinic acid.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00201337
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and biochemical characterization of heparin-binding proteins from boar seminal plasma: A dual role for spermadhesins in fertilization (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 35 (1993), S. 37-43 
    Details
    ISSN: 1040-452X
    Keywords: Boar seminal plasma ; Heparin-binding proteins ; Capacitation factors ; Spermadhesins ; Fertilization ; N-terminal sequence ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Sperm surface-coated heparin-binding proteins originating from secretions of the male sexual accessory glands, are known to play a pivotal role as extrinsic regulatory factors during sperm capacitation in many mammalian species. They interact with glycosaminoglycans present in the female genital tract and enhance the subsequent zona pellucida-induced acrosome reaction. We have isolated heparin-binding proteins from boar seminal plasma by affinity chromatography on heparin-Sepharose and reverse-phase HPLC. N-Terminal sequence analysis of these proteins identified a boar counterpart of the bovine capacitation factors BSP-A1/2 (also called PDC-109) and BSP-A3. Several carbohydrate- and zona pellucida-binding proteins, which belong to the newly described spermadhesin family, were also identified as heparin-binding proteins. Our results imply that, besides other capacitation factors, members of the spermadhesin family may play a dual role in sperm capacitation and fertilization in the pig. © 1993 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080350107
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  • 4
    Electronic Resource
    Electronic Resource
    Differential protective effects of O-phenanthroline and catalase on H2O2-induced DNA damage and inhibition of protein synthesis in endothelial cells (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 149 (1991), S. 408-413 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The respective roles of H2O2 and ·OH radicals was assessed from the protective effects of catalase and the iron chelator o-phenanthroline on (1) the inhibition of protein synthesis, and (2) DNA damage and the related events (activation of the DNA repairing enzyme poly(ADP) ribose polymerase with the associated depletion of NAD and ATP stores) in cultured endothelial cells exposed to the enzyme reaction hypoxanthine-xanthine oxidase (HX-XO) or pure H2O2. Catalase added in the extracellular phase completely prevented all of these oxidant-induced changes. O-phenanthroline afforded a complete protective effect against DNA strand breakage and the associated activation of the enzyme poly(ADP) ribose polymerase. By contrast, iron chelation was only partially effective in maintaining the cellular NAD and ATP contents, as well as the protein synthetic activity. In addition, the ATP depletion following oxidant injury was much more profound than NAD depletion. These results indicate that: (1) ·OH radical was most likely the ultimate O2 species responsible for DNA damage and activation of poly-(ADP) ribose polymerase; (2) both H2O2 and ·OH radicals were involved in the other cytotoxic effects (inhibition of protein synthesis and reduction of NAD and ATP stores); and (3) NAD and ATP depletion did not result solely from activation of poly(ADP) ribose polymerase, but other mechanisms are likely to be involved. These observations are also compatible with the existence of a compartmentalized intracellular iron pool.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041490308
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of butylated hydroxytoluene on biliineage differentiation of the human HL-60 myeioblastic leukemia cell (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 144 (1990), S. 36-41 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Butylated hydroxytoluene (BHT), which has both antioxidant and membrane active properties, has been reported to affect cellular differentiation. We studied its effect on the bipotent lineage differentiation of the important HL-60 human my-eloblastic leukemia cell line using reduction of nitroblue tetrazolium, cell cycle analysis, population growth rote, monoclonal antibodies, and morphology. BHT markedly accelerated retinoic acid-induced myelocytic differentiation and dihydroxyvitamin D3-induced monocvtic differentiation in a concentration and time-dependent manner. Butylated hydroxyanisole (BHA) had a comparable effect. Preincubation with the compounds was not necessary to evoke the acceleration. Other antioxidants and inhibitors of eicosanoid synthesis were inactive. We conclude that the important food preservatives BHT and BHA accelerate the kinetics of terminal differentiation of human leukemia and that this effect is likely due at least in part to their membrane active properties.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041440106
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  • 6
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    Carcinogenicity of chloroform (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Messing, R B -- Gust, L D -- Petersen, D W -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1518-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202700" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Carcinogenicity Tests ; Chloroform/administration & dosage/*toxicity ; Female ; Humans ; Kidney Neoplasms/*chemically induced ; Rats ; Risk Factors ; *Water Supply
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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