ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Differences in tissue expressions of enzyme activities in interspecific sunfish (Centrarchidae) hybrids and their backcross progeny (1984)
    Springer
    Biochemical genetics 22 (1984), S. 931-956 
    Details
    ISSN: 1573-4927
    Keywords: interspecific hybrids ; fish ; enzyme locus expression ; tissue enzyme activities ; malate dehydrogenase ; lactate dehydrogenase ; glucosephosphate isomerase ; phosphoglucomutase ; developmental regulation ; gene regulatory evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The extent of naturally occurring variations of enzyme locus expression was determined for three tissues (liver, muscle, and eye) in two species of sunfish (Centrarchidae), the green sunfish (Lepomis cyanellus) and the redear sunfish (L. microlophus). The genetic basis for species differences in tissue enzyme specific activities of malate dehydrogenase (EC 1.1.1.37), lactate dehydrogenase (EC 1.1.1.27), phosphoglucomutase (EC 2.7.5.1), and glucosephosphate isomerase (EC 5.3.1.9) was investigated by determining enzyme specific activities in the tissues of the reciprocal F1 hybrids and of their backcross progenies. The specific activities for most enzymes in hybrids were intermediate between those of the parental species. Significant differences in enzyme specific activity were detected among the F1 progeny as well as those of backcrosses. Variations in specific activity levels in one tissue were often independent of variations in specific activities in a different tissue. However, the changes in the specific activities of different enzymes within the same tissue were often positively correlated. The tissue glucosephosphate isomerase activity differences appear not to be due to different functional contributions of the glucosephosphate isomerase allelic isozymes. Cluster analysis of distributions of specific activities revealed no simple Mendelian pattern of inheritance for control of tissue enzyme activity. Our results suggest a polygenic control of tissue enzyme specific activity levels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00499484
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Desmosome assembly in MDCK epithelial cells does not require the presence of functional microtubules (1992)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 23 (1992), S. 201-212 
    Details
    ISSN: 0886-1544
    Keywords: intercellular junctions ; desmosome ; assembly ; microtubules ; epithelia ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Desmosomes, complex multisubunit structures that assemble at sites of cell-cell contact, are important components of the epithelial junctional complex. Desmosome assembly requires the coordinated interaction at the plasma membrane of at least 8 cytoplasmic and integral membrane proteins organized into two structurally and functionally distinct domains, the cytoplasmic plaque and membrane core. Previous studies (Pasdar et al., J. Cell Biol., 113:645-655) provided evidence that cytokeratin filaments and microtubules may regulate transfer and assembly of cytoplasmic plaque and membrane core proteins, respectively. To determine directly the role of microtubules in these processes, Madin-Darby canine kidney (MDCK) cells were treated with nocodazole or colchicine to disrupt the microtubular network. Biochemical analysis of the different components of the cytoplasmic plaque and membrane core domains revealed little or no effect of nocodazole or colchicine on the kinetics of synthesis, post-translational modifications, transfer of proteins to the plasma membrane or their metabolic stability in the presence or absence of cell-cell contact. Likewise, immunofluorescence analysis of desmosome formation demonstratedan apparently normal desmosome assembly in the presence of nocodazole or colchicine upon induction of cell-cell contact. These results indicate that an intact microtubular network is not necessary for the processing or transport of the desmosomal membrane core glycoproteins to the plasma membrane in the absence or presence of cell-cell contact. Furthermore, the integration of the cytoplasmic plaque and membrane core domains induced by cell-cell contact at the plasma membranes of adjacent cells does not require the presence of functional microtubules. © 1992 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970230304
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Desmosome assembly and disassembly are regulated by reversible protein phosphorylation in cultured epithelial cells (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 108-121 
    Details
    ISSN: 0886-1544
    Keywords: intercellular junctions ; desmosome ; assembly ; kinase ; phosphatase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Desmosomes are one component of the intercellular junctional complex in epithelia. In cultures of epithelial cells, desmosome assembly can be regulated by modulating the calcium concentrations of the growth media. At present, very little is known about the intracellular signal transduction mechanisms that regulate desmosome assembly and disassembly in response to changing extracellular calcium concentrations. We have used inhibitors of protein kinases and phosphatases in a combined biochemical and morphological approach to analyze the role of protein phosphorylation in the assembly and disassembly of desmosomes in Madin-Darby canine kidney epithelial cells. Our results suggest that desmosomal proteins (desmoplakins I/II and desmoglein 1) are primarily phosphorylared on serine residues. Electron microscopic analyses of desmosome assembly upon induction of cell-cell contact, in the presence of protein kinase inhibitor, H-7, revealed an apparently normal assembly of desmosomes. However, complete disassembly of desmosomes was inhibited by H-7 upon removal of extracellular calcium. Under these conditions, although desmosomes split, desmosomal plaques and their associated cytokeratin filaments can not be internalized. In contrast, treatment of the cultures with okadaic acid (OA), an inhibitor of protein phosphatases, inhibited desmosome assembly but had no effect on disassembly. In addition, the inhibitory effect of okadaic acid on desmosome assembly was specific to this junction since we observed apparently normal tight junction and adherens junction in okadaic acid-treated cultures. These results suggest that via reversible protein phosphorylation involving both protein kinase and protein phosphatases. © 1995 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970300203
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Plakoglobin: Kinetics of synthesis, phosphorylation, stability, and interactions with desmoglein and E-cadherin (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 258-272 
    Details
    ISSN: 0886-1544
    Keywords: adhering junctions ; desmosome ; assembly ; phosphorylation ; protein interaction ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have analyzed the kinetics of synthesis, phosphorylation, and stability of the soluble and insoluble plakoglobin (PG) and their interactions with Dsg1 and E-cadherin in Madin-Darby canine kidney (MDCK) epithelial cells in the absence of cell adhesion and after the induction of cell-cell contact. Using a combination of biochemical and morphological approaches, we show that newly synthesized PG enters a soluble:insoluble pool of proteins in a 60:40 ratio regardles of cell-cell contact. Following synthesis, PG is increasingly found in the insoluble pool. Although cell-cell contact does not effect either the size of each pool or the rate or efficiency of the transfer from the soluble into the insoluble pool, it results in a significant increase in the metabolic stability of the newly synthesized insoluble PG. The soluble PG initially forms separate complexes with E-cadherin and Dsg1. PG-Dsg1 complexes become insoluble and localize to the desmosome. PG-E-cadherin complexes remain soluble and are distributed intracellularly. The insoluble PG and E-cadherin detected at the cell periphery remain distinctly separate, as demonstrated previously [Hinck et al., 1994: J. Cell Biol. 125:1327-1340; Nathke et al., 1994: J. Cell Biol. 125:1341-1352]. In addition, we detected a separate pool of PG which is not associated with either Dsg1 or E-cadherin and after the induction of cell-cell contact becomes primarily insoluble and is distributed along the lateral membrane. Phoshorylation analysis showed that there is a significantly greater amount of phosphorylated PG in the soluble pool than in the insoluble pool. In addition the soluble pool is both serine and theronine phosphorylated, whereas the insoluble PG is primarily phosphorylated on serine residues. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320403
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Disorganization of microfilaments and intermediate filaments interferes with the assembly and stability of desmosomes in MDCK epithelial cells (1993)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 26 (1993), S. 163-180 
    Details
    ISSN: 0886-1544
    Keywords: intercellular junctions ; desmosome ; assembly ; MDCK ; epithelia ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: To investigate the possible role(s) of cytoskeletal elements in desmosome assembly we have studied the effects of cytostatic drugs on the assembly of desmosomes in MDCK epithelial cells. We showed previously [Pasdar et al.: Cell Motil. Cytoskeleton 23:201-213, 1992] that selective disruption of microtubules has no effect on desmosome assembly. Here, we have treated MDCK cells with cytochalasin B and a combination of cytochalasin B and nocodazole and analysed the effects on desmosome assembly. Immunofluorescence analysis of MDCK cultures following drug treatment indicated complete disruption of actin microfilaments and disorganization of cytokeratin intermediate filaments. Biochemical analysis of newly synthesized desmosomal membrane core glycoproteins as well as the cell adhesion proteir. E-cadherin revealed no effect of these drugs on the kinetics of synthesis, intracellular processing, or transport to the plasma membrane either in the presence or absence of cell-cell contact. However, morphological analyses revealed a significant disruption in the spatial organization of desmosomal proteins and E-cadherin. Drug treatment in the absence of cell-cell contact resulted in the disruption of the normally observed homogenous punctate staining pattern and appearance of aggregate staining. Induction of cell-cell contact in these cultures resulted in redistribution of some of the aggregate staining to the plasma membrane. In contrast to control cultures, significant amount of intracellular staining was retained for all desmosomal proteins. Biochemical analyses of turnover rates of newly synthesized desmosomal proteins indicated a significant decrease in metabolic stability of these proteins while the turnover rate of E-cadherin was not significantly different among control and drug-treated cultures. Taken together, these results suggest that intact actin and cytokeratin filaments are necessary for the stability, efficient assembly, and spatial organization of the junctional components at the membrane. The regulatory role of cytokeratins and actin filaments in assembly and stability of desmosomes on the plasma membrane is discussed. © 1993 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970260207
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    facet.materialart.
    Unknown
    Pattern Similarity Analysis of Amino Acid Sequences for Peptide Emulsification (2004)
    American Chemical Society
    Details
    Publication Date: 2004-02-01
    Print ISSN: 0021-8561
    Electronic ISSN: 1520-5118
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Published by American Chemical Society
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 7
    facet.materialart.
    Unknown
    Poly[tri-μ2-aqua-(μ3-pyridine-2,4-dicarboxylato-κ4N,O2:O2:O2′)barium] (2011)
    International Union of Crystallography (IUC)
    Details
    Publication Date: 2011-06-04
    Description: In the polymeric title compound, [Ba(C7H3NO4)(H2O)3]n, the BaII ion is ten-coordinated in an NO9 environment by one N atom and three O atoms from three pyridine-2,4-dicarboxylate (pydc) ligands and six water molecules. The μ3-pydc ligands and the bridging water molecules connect the Ba atoms into a layer parallel to (100). The crystal packing is stabilized by O—H...O and C—H...O hydrogen bonds.
    Electronic ISSN: 1600-5368
    Topics: Chemistry and Pharmacology , Geosciences
    Published by International Union of Crystallography (IUC)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 8
    facet.materialart.
    Unknown
    catena-Poly[[[(2,2′-bipyridine-κ2N,N′)(dimethyl sulfoxide-κO)(nitrato-κ2O,O′)bismuth(III)]-μ-5-carboxybenzene-1,3-dicarboxylato-κ4O1,O1′:O3,O3′] dimethyl sulfoxide monosolvate] (2011)
    International Union of Crystallography (IUC)
    Details
    Publication Date: 2011-02-20
    Description: The polymeric title compound, {[Bi(C9H4O6)(NO3)(C10H8N2)(C2H6OS)]·C2H6OS}n, was obtained by the reaction of bismuth(III) nitrate, bipyridine (bpy) and 1,3,5-benzenetricarboxylic acid (H3BTC). The BiIII ion is coordinated in a distorted tricapped trigonal-prismatic geometry, defined by two N atoms of the bipy ligand, four O atoms of two HBTC2− anions, two O atoms of a nitrate anion and one O atom of a dimethyl sulfoxide ligand. The crystal packing is stabilized by O—H...O and C—H...O hydrogen bonds. The S atom of the non-coordinating dimethyl sulfoxide molecule is disordered over two sets of sites with refined site-occupancies of 0.430 (19) and 0.570 (19).
    Electronic ISSN: 1600-5368
    Topics: Chemistry and Pharmacology , Geosciences
    Published by International Union of Crystallography (IUC)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 9
    facet.materialart.
    Unknown
    Bis(2-amino-6-methylpyridinium) tris(pyridine-2,6-dicarboxylato)zirconate(IV) dihydrate (2011)
    International Union of Crystallography (IUC)
    Details
    Publication Date: 2011-02-03
    Description: In the title compound, (C6H9N2)2[Zr(C7H3NO4)3]·2H2O, the ZrIV atom is nine-coordinated by three pyridine-2,6-dicarboxylate ligands in a distorted tricapped trigonal–prismatic ZrN3O6 environment. The crystal packing is stabilized by intermolecular N—H...O and O—H...O hydrogen bonds.
    Electronic ISSN: 1600-5368
    Topics: Chemistry and Pharmacology , Geosciences
    Published by International Union of Crystallography (IUC)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 10
    facet.materialart.
    Unknown
    Benzene-1,3-diammonium bis(pyridine-2,6-dicarboxylato-κ3O2,N,O6)cobaltate(II) pentahydrate (2011)
    International Union of Crystallography (IUC)
    Details
    Publication Date: 2011-04-01
    Description: In the title compound, (C6H10N2)[Co(C7H3NO4)2]·5H2O, the CoII ion is six-coordinated in an N2O4 environment by two pyridine-2,6-dicarboxylate (pydc) ligands, having a distorted octahedral geometry. The crystal packing is stabilized by intermolecular N—H...O, O—H...O and weak C—H...O hydrogen bonds. There are also π–π interactions between the pyridine rings of the pydc ligands and between the pydc ligands and the benzene-1,3-diammonium cations, with centroid–centroid distances of 3.4575 (15) and 3.7521 (15) Å.
    Electronic ISSN: 1600-5368
    Topics: Chemistry and Pharmacology , Geosciences
    Published by International Union of Crystallography (IUC)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...