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  • 1
    Electronic Resource
    Electronic Resource
    PRELIMINARY ESTIMATES OF THE DOPAMINE β-HYDROXYLASE CONTENT AND ACTIVITY IN PURIFIED NORADRENERGIC VESICLES (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 28 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The dopamine β-hydroxylase (DβH) content and activity of large dense-core noradrenergic vesicles purified from bovine splenic nerve were determined using two assay procedures : enzymic activity expressed in Units per mg protein and homospecific activity based on radioimmunoassay expressed in Units per mg DβH antigen. Approximately two-thirds of the total enzyme activity is latent in these vesicles, even after various treatments designed to compromise vesicle integrity. DβH can be completely unmasked by brief treatment with 0.01-0.05% Triton X-100 and activity increases from 0.20 to 0.64 Units per mg vesicle protein. Calculations based on both assay methods suggested that an average of 7% (range 3-15%) of the total vesicle protein was DβH and that the average vesicle contained about 4 molecules of enzyme (range 2-9 molecules). The estimated homospecific activities indicated an average of 25 and 50% (range 18-72%) of the vesicle enzyme was inactive in the various samples using the two antibodies. The vesicle can synthesize up to 30 molecules of noradrenaline/s per molecule of DβH at near optimal substrate concentration, and 60-270 molecules of norepinephrine/s per vesicle. The assumptions used in the various calculations were critically analyzed and, based on the methods employed, it is tentatively considered to be unlikely that there could be more than 5-12 molecules of DβH per vesicle. The possibility that circulating DβH originates primarily, if not exclusively, from the large dense-core vesicle type is considered and the functional implications of the data support the concept of vesicle reuse during several cycles of exocytosis involving a quantal size equal to a fraction of the vesicle transmitter content.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb07711.x
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  • 2
    Electronic Resource
    Electronic Resource
    The archaeal halophilic virus-encoded Dam-like methyltransferase M.φCh1-I methylates adenine residues and complements dam mutants in the low salt environment of Escherichia coli (2000)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 35 (2000), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The genome of the archaeal virus φCh1, infecting Natrialba magadii (formerly Natronobacterium magadii), is composed of 58.5 kbp linear ds DNA. Virus particles contain several RNA species in sizes of 100–800 nucleotides. A fraction of φCh1 genomes is modified within 5′-GATC-3′ and related sequences, as determined by various restriction enzyme digestion analyses. High performance liquid chromatography revealed a fifth base, in addition to the four nucleosides, which was identified as N6-methyladenosine. Genetic analyses and subsequent sequencing led to the identification of a DNA (N6-adenine) methyltransferase (mtase) gene. The protein product was designated M.φCh1-I. By the localization of the most conserved motifs (a DPPY motif occurring before FxGxG), the enzyme was placed within the β-subgroup of the (N6-adenine) methyltransferase class. The mtase gene of φCh1 was classified as a ‘late’ gene, as determined by measuring the kinetics of mRNA and protein expression in N. magadii during the lytic cycle of φCh1. After infection of cells, M.φCh1-I mRNA and protein could be detected in lower amounts than in the situation of virus induction from lysogenic cells. Consequently, only about 5% of the φCh1 progeny genomes after infection of N. magadii carry the M.φCh1-I methylation in contrast to 50% of virus genomes generated by induction of φCh1-lysogenic N. magadii cells. Heterologous expression of the mtase from a halophile with 3 M cytoplasmic salt concentration showed an unexpected feature: the protein was active in the low environment of Escherichia coli and was able to methylate DNA in vivo. Interestingly, it seemed to exhibit a higher sequence specificity in E. coli that resulted in adenine methylation exclusively in the sequence 5′-GATC-3′. Additionally, expression of M.φCh1-I in dam–E. coli cells led to a complete substitution of the function of M.Dam in DNA mismatch repair.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2000.01786.x
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  • 3
    Electronic Resource
    Electronic Resource
    Inversion within the haloalkaliphilic virus φCh1 DNA results in differential expression of structural proteins (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 52 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The sequence of φCh1 contains an open reading frame (int1) in the central part of its genome that belongs to the λ integrase family of site-specific recombinases. Sequence similarities to known integrases include the highly conserved tetrad R-H-R-Y. The flanking sequences of int1 contain several direct repeats of 30 bp in length (IR-L and IR-R), which are orientated in an inverted direction. Here, we show that a recombination active region exists in the genome of φCh1: the number of those repeats, non-homologous regions within the repeat clusters IR-L and IR-R and the orientation of the int1 gene vary in a given virus population. Within this study, we identified circular intermediates, composed of the int1 gene and the inwards orientated repeat regions IR-L and IR-R, which could be involved in the recombination process itself. IR-L and IR-R are embedded within ORF34 and ORF36 respectively. As a consequence of the inversion within this region of φCh1, the C-terminal parts of the proteins encoded by ORF34 and 36 are exchanged. Both proteins, expressed in Escherichia coli, interact with specific antisera against whole virus particles, indicating that they could be parts of φCh1 virions. Expression of the protein(s) in Natrialba magadii could be detected 98 h after inoculation, which is similar to other structural proteins of φCh1. Taken together, the data show that the genome of φCh1 contains an invertible region that codes for a recombinase and structural proteins. Inversion of this segment results in a variation of these structural proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2003.03983.x
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  • 4
    Electronic Resource
    Electronic Resource
    Natrialba magadii virus φCh1: first complete nucleotide sequence and functional organization of a virus infecting a haloalkaliphilic archaeon (2002)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 45 (2002), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The double-stranded (ds)DNA virus φCh1 infects the haloalkaliphilic archaeon Natrialba magadii. The complete DNA sequence of 58 498 bp of the temperate virus was established, and the probable functions of 21 of 98 φCh1-encoded open reading frames (ORFs) have been assigned. This knowledge has been used to propose functional modules each required for specific functions during virus development. The φCh1 DNA is terminally redundant and circularly permuted and therefore appears to be packaged by the so-called headful mechanism. The presence of ORFs encoding homologues of proteins involved in plasmid replication as well as experimental evidence indicate a plasmid-mediated replication strategy of the virus. Results from nanosequencing of virion components suggest covalent cross-linking of monomers of at least one of the structural proteins during virus maturation. A comparison of the φCh1 genome with the partly sequenced genome of Halobacterium salinarum virus φH revealed a close relationship between the two viruses, although their host organisms live in distinct environments with respect to the different pH values required for growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2002.03064.x
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  • 5
    Electronic Resource
    Electronic Resource
    Variations of sperm release in three batches of zebrafish (2004)
    Oxford, UK; Malden , USA : Blackwell Science Ltd
    Journal of fish biology 64 (2004), S. 0 
    Details
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: By collecting and counting the number of sperm released during separate matings in three batches of zebrafish Danio rerio, aged 3–4, 4–5 and 5–6 months, males were observed to release sperm before the female started laying their eggs. After the female left the nest, the number and motility of sperm and life span of sperm of younger fish were higher than those of older fish in water samples collected under the nest and at the surface of the tank. Sperm were released in the form of sperm trails laid on the nest surface, subsequently active spermatozoa left the trails and moved in the water for several minutes. Sperm trails consisted of bands of viscous material in which the sperm were embedded. In most cases eggs were not laid directly over the sperm trail, suggesting that sperm may contact the eggs after the latter are released into the water. In all the three tested groups there was no significant difference (P 〉 0·05) between the number of sperm collected on some portions of the acetate sheets which lined the nest ceiling. This result demonstrated that the greater activity of younger fish accelerated the sperm dispersal in water. Male sperm duct glands, seminal vesicles, known to secrete mucosubstances are probably involved in the production of sperm trails. The possible influence of insemination on the mating style of zebrafish is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0022-1112.2004.00315.x
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  • 6
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    Effects of stress on attachment behavior in infants (1978)
    Provincetown, Mass., etc. : Periodicals Archive Online (PAO)
    The Journal of Genetic Psychology. 132:2 (1978:June) 321 
    Details
    ISSN: 0022-1325
    Topics: Psychology
    Notes: REPLICATIONS AND REFINEMENTS
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:3284-1978-132-02-000021
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  • 7
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    PATTERNS OF CORTICAL BONE GROWTH IN MODERATELY MALNOURISHED PRESCHOOL CHILDREN (1975)
    Baltimore : Periodicals Archive Online (PAO)
    Human Biology. 47:3 (1975:Sept.) 337 
    Details
    ISSN: 0018-7143
    Topics: Biology
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:5243-1975-047-03-000010
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  • 8
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    MALNUTRITION, BODY SIZE, AND SKELETAL MATURATION: INTERRELATIONSHIPS AND IMPLICATIONS FOR CATCH-UP GROWTH (1979)
    Baltimore : Periodicals Archive Online (PAO)
    Human Biology. 51:3 (1979:Sept.) 371 
    Details
    ISSN: 0018-7143
    Topics: Biology
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:5243-1979-051-03-000009
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  • 9
    Electronic Resource
    Electronic Resource
    Nuclear Membrane Hydrolysis of Adenosine Triphosphate (1966)
    [s.l.] : Nature Publishing Group
    Nature 212 (1966), S. 609-609 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Ultramicrotome sections were taken from the region immediately below the surface of the tissue, which was post fixed in 1 per cent osmium tetroxide and embedded in 'Epon'. Electron micrographs were taken with a 'Siemens Elmiskop P. Fig. 1 shows a section taken from an experimental 4 day embryonic ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/212609a0
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  • 10
    Electronic Resource
    Electronic Resource
    A longitudinal study of autoantibodies against central nervous system tissue and gangliosides in connective tissue diseases (2000)
    Springer
    Rheumatology international 19 (2000), S. 83-88 
    Details
    ISSN: 1437-160X
    Keywords: Key words Connective tissue diseases ; Longitudinal ; Neuropsychiatric ; Antibodies against central nervous tissue ; Gangliosides antibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Our objective was to investigate longitudinally, antibodies against central nervous tissue (anti-CNS) derived from bovine brain and gangliosides GM1, GD1a, GD1b, and GT1b in 91 patients with connective tissue diseases (systemic lupus erythematosus, n=38; mixed connective tissue disease, n=16; primary Sjögren's syndrome, n=7; progressive systemic sclerosis, n=13; polymyositis/dermatomyositis, n=4; overlap syndrome, n=5; undifferentiated connective tissue disease, n=8). Anti-CNS and anti-ganglioside antibodies, measured by enzyme-linked immunosorbent assay, were found in 73% and 63% of patients, respectively. Anti-CNS positive sera were also reactive in Western blotting in 74% of cases and recognized up to 14 different polypeptides from 29 to 130 kDa. Anti-CNS and anti-ganglioside antibodies reflected only in a limited extent the disease activity. In 27 of 58 patients, anti-CNS antibodies remained positive independently of disease activity and antibody levels did not correlate with the phases of exacerbations. A total of 36 of 60 anti-CNS-positive patients, in contrast to two of 22 anti-CNS-negative patients, had major neuropsychiatric manifestations (P 〈 0.001). Anti-ganglioside antibodies were not significantly associated with neuropsychiatric manifestations. In conclusion, our longitudinal data suggest that anti-CNS antibodies may be an important marker for the diagnosis of cerebral involvement in connective tissue diseases, but the pathogenic role of these autoantibodies remains to be determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002960050108
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