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  • 1
    Electronic Resource
    Electronic Resource
    Histochemical investigation of β-glucuronidase in culture cells and regenerated plants of Scutellaria baicalensis Georgi (2000)
    Springer
    Plant cell reports 19 (2000), S. 390-394 
    Details
    ISSN: 1432-203X
    Keywords: Key words Scutellaria ; Callus culture ; Regeneration ; β-Glucuronidase ; Distribution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Strong activity of β-glucuronidase first appeared in the epidermal and glandular hair cells of leaf primordia regenerated from callus of Scutellaria baicalensis Georgi. Leaf primordia matured rapidly in culture to form shoots within 1 month in which both the mesophyll cells and the glandular hairs were deeply stained. Leaves predominantly accumulated β-glucuronidase in both glandular hair cells and mesophyll cells. β-Glucronidase activity in leaves was higher in the summer and decreased in the winter. The stem section collected in the summer had a different β-glucuronidase distribution pattern from that of the root in that in the former strong activity appeared in the periderm cells and collenchyma cells which was decreasingly dispersed into the phloem layer cells. In the winter, β-glucronidase activity decreased compared to that in summer. It can be argued that the distribution of β-glucuronidase in this plant is closely linked with the defense against pathogens: it is a starting key enzyme which may act together with the flavonoids, which play an important role as a proton donor for the detoxification metabolism of H2O2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002990050745
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Biosynthesis of prostaglandins by human spermatozoa in vitro and their role in acrosome reaction and fertilization (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 33 (1992), S. 303-306 
    Details
    ISSN: 1040-452X
    Keywords: Arachidonic acid ; Calcium ionophores ; Cyclooxygenase ; Cyclooxygenase inhibitors ; Lipoxygenase products ; Phospholipase A2 ; Thromboxanes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Five homogenates of human sperm cells were separately incubated with [14C]arachidonic acid in the presence of reduced glutathione, L-tryptophan, and haematin as cofactors. The cyclooxygenase products of archidonic acid metabolism were extracted, separated, and measuréd for their radioactivity. The rate of formation of prostaglandin (PG)D2, PGE2, PGF2α, 6-keto PGF1α, and thromboxane (TX)B2 were 18.0 ± 1.11, 10.9 ± 0.68, 5.8 ± 0.21, 3.9 ± 0.13 and 6.6 ± 0.52 pmol/106 cells/min, respectively. These results are discussed in relation to the hypothesis that cyclooxygenase metabolites of certain polyunsaturated fatty acids play an important part in the sperm acrosome reaction and fertilization. © 1992 Wiley-Liss, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080330311
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  • 3
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    Structure of a prehandover mammalian ribosomal SRP{middle dot}SRP receptor targeting complex (2018)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2018-04-20
    Description: Signal recognition particle (SRP) targets proteins to the endoplasmic reticulum (ER). SRP recognizes the ribosome synthesizing a signal sequence and delivers it to the SRP receptor (SR) on the ER membrane followed by the transfer of the signal sequence to the translocon. Here, we present the cryo–electron microscopy structure of the mammalian translating ribosome in complex with SRP and SR in a conformation preceding signal sequence handover. The structure visualizes all eukaryotic-specific SRP and SR proteins and reveals their roles in stabilizing this conformation by forming a large protein assembly at the distal site of SRP RNA. We provide biochemical evidence that the guanosine triphosphate hydrolysis of SRP·SR is delayed at this stage, possibly to provide a time window for signal sequence handover to the translocon.
    Keywords: Molecular Biology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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