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  • 1
    Digitale Medien
    Digitale Medien
    Characterization of the bip gene of Aspergillus awamori encoding a protein with an HDEL retention signal homologous to the mammalian BiP involved in polypeptide secretion (1997)
    Springer
    Current genetics 32 (1997), S. 139-146 
    Details
    ISSN: 1432-0983
    Schlagwort(e): Key words Protein secretion ; Fungi ; BiP protein ; Endoplasmic reticulum
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract A DNA fragment containing an open reading frame of 2016 nucleotides has been cloned from the DNA of Aspergillus awamori by hybridization with a probe internal to the KAR2 (BiP) gene of Saccharomyces cerevisiae. The 73.4-kDa-encoded protein showed very high similarity to the endoplasmic reticulum (ER) lumenal BiP protein of S. cerevisiae, Kluyveromyces lactis, Schizosaccharomyces pombe, and animal and plant cells. The BiP protein contains a polar N-terminal end followed by a 18-amino-acid strongly hydrophobic region corresponding to the leader peptide for transport through the ER membrane. In the C-terminal region the protein ends with the HDEL canonical ER retention signal that targets proteins to the lumen of the ER. The A. awamori bip gene contains three introns as shown by cloning and sequencing the putative intron regions from a cDNA library. The bip gene is transcribed as a monocistronic mRNA of 2.4 kb. Two transcription start sites located 160 and 233 bp upstream of the first translated ATG were identified by primer extension. The promoter region showed no consensus TATA box but it contains CCAAT and CreA boxes known to be involved in both stress and carbon-catabolite regulation of fungal promoters.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s002940050258
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Immunocytochemical localization of allergenic protein (Ole e I) in the endoplasmic reticulum of the developing pollen grain of olive (Olea europaea L.) (1995)
    Springer
    Planta 196 (1995), S. 558-563 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Allergenic protein (immunolocalization) ; Endoplasmic reticulum ; Olea ; Pollen (olive)
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The monoclonal antibody OL-1 and transmission electron microscopy were used to locate immunologically the major allergen of olive pollen. Ole e I, during pollen grain development. Within the pollen grain, allergenic proteins are located in the cisternae of the rough endoplasmic reticulum. Our findings indicate that the synthesis of these proteins starts in the vegetative cytoplasm of olive pollen during the early maturation stage.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00203656
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Endoplasmic reticulum as a storage site for allergenic proteins in pollen grains of several Oleaceae (1995)
    Springer
    Protoplasma 187 (1995), S. 111-116 
    Details
    ISSN: 1615-6102
    Schlagwort(e): Allergenic protein ; Oleaceae ; Pollen ; Endoplasmic reticulum ; Immuno-localization ; Ultrastructure
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary The ultrastructure of mature pollen grains of several Oleaceae species (Olea europaea, Fraxinus excelsior, Syringa vulgaris, Ligustrum vulgare, andForsythia suspensa) was studied and the immunolocalization of Ole e I, the major allergen of olige pollen, was determined by immunogold labelling. The five Oleaceae pollens studied here showed different intensities of labelling. The Ole e I allergen was localized throughout the rough endoplasmic reticulum. The absence of gold particles in other cell compartments, such as nuclei, pastids, mitochondria, dictyosomes, lipid bodies, and cell wall, as well as the absence of labelling in control preparations, indicate the specificity of immunolocalization. We conclude that endoplasmic reticulum of the mature pollen grain is a storage site for allergenic proteins and is probably also involved in their synthesis.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01280238
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  • 4
    Digitale Medien
    Digitale Medien
    High resolution density gradient electrophoresis of cellular organelles (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 173-178 
    Details
    ISSN: 0173-0835
    Schlagwort(e): Separation of cellular organelles ; Endosomes ; Lysosomes ; Endoplasmic reticulum ; Plasma membrane ; Density gradient electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: A density gradient electrophoresis apparatus made of Perspex was constructed, with a separation column (7 × 2.2 cm) containing a 0-5% linear Ficoll gradient. The useful separation path is 6 cm. A specially designed gradient mixer is described which fits over the application cone. This cone permits precise gradient and sample introduction as well as undisturbed fractionation after electrophoresis. A bottom circular palladium cathode is separated hydrodynamically but not electrically from the density gradient by a cellophane membrane, merely secured by an O-ring. The top circular platium anode allows for upward electrophoresis (80-100 min at 10 mA). The markedly higher resolution of subcellular organelles was compared with separations obtained earlier with a small, but much more difficult to fabricate, prototype. Moreover, ease of manipulation was greatly improved. A wide separation distance was obtained between plasma membrane, endoplasmatic reticulum as well as between two populations of lysosomes. Even early, middle, and late endosomes could be separated with high resolution. Soluble isoenzymes could be separated as well and were far away from the vesicle-enclosed enzymes.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/elps.1150170128
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  • 5
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    Unbekannt
    Molecular cloning and disease association of hepatitis G virus: a transfusion-transmissible agent (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1996-01-26
    Beschreibung: An RNA virus, designated hepatitis G virus (HGV), was identified from the plasma of a patient with chronic hepatitis. Extension from an immunoreactive complementary DNA clone yielded the entire genome (9392 nucleotides) encoding a polyprotein of 2873 amino acids. The virus is closely related to GB virus C (GBV-C) and distantly related to hepatitis C virus, GBV-A, and GBV-B. HGV was associated with acute and chronic hepatitis. Persistent viremia was detected for up to 9 years in patients with hepatitis. The virus is transfusion-transmissible. It has a global distribution and is present within the volunteer blood donor population in the United States.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linnen, J -- Wages, J Jr -- Zhang-Keck, Z Y -- Fry, K E -- Krawczynski, K Z -- Alter, H -- Koonin, E -- Gallagher, M -- Alter, M -- Hadziyannis, S -- Karayiannis, P -- Fung, K -- Nakatsuji, Y -- Shih, J W -- Young, L -- Piatak, M Jr -- Hoover, C -- Fernandez, J -- Chen, S -- Zou, J C -- Morris, T -- Hyams, K C -- Ismay, S -- Lifson, J D -- Hess, G -- Foung, S K -- Thomas, H -- Bradley, D -- Margolis, H -- Kim, J P -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):505-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genelabs Technologies, Redwood City, CA 94063, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560265" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acute Disease ; Amino Acid Sequence ; Base Sequence ; Blood Donors ; Blood Transfusion/*adverse effects ; Blood-Borne Pathogens ; Chronic Disease ; Cloning, Molecular ; Consensus Sequence ; Disease Transmission, Infectious ; Flaviviridae/genetics ; Genome, Viral ; Hepatitis Viruses/chemistry/*genetics/isolation & purification ; Hepatitis, Viral, Human/epidemiology/transmission/*virology ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA Viruses/chemistry/*genetics/isolation & purification ; RNA, Viral/blood/genetics ; Sequence Alignment ; United States/epidemiology ; Viral Proteins/chemistry/genetics ; Viremia/epidemiology/virology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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