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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 12581-12591 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 16 (1977), S. 1857-1865 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of biomedical science 7 (2000), S. 169-172 
    ISSN: 1423-0127
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 304 (1983), S. 485-486 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] To many cell biologists trying to understand how cytoskeletal filamentsinteract with cell surfaces, skeletal muscle cells seem to be less attractive than popular non-musclemembrane systems such as the erythrocyte membrane skeleton1, the brush border of intestinal epithelial cells2 and the adhesion ...
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  • 5
    ISSN: 1572-9729
    Keywords: hydrofluorocarbons ; hydrochlorofluorocarbons ; methanotrophs ; biotransformations ; cometabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Energy, Environment Protection, Nuclear Power Engineering , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract This research investigated the potential for methanotrophic biotransformation of three HCFCs — chlorodifluoromethane (HCFC-22); 1-chloro-1,1-difluoroethane (HCFC-142b); and 1,1-dichloro-2,2,2-trifluoroethane (HCFC-123); and one HFC — 1,2,2,2-tetrafluoroethane (HFC-134a). All of these compounds were biotransformed to differing degrees by methanotrophic mixed culture MM1. Rates of transformation were obtained by monitoring disappearance of the target compounds from the headspace in batch experiments. Henry's constants were determined over a range of conditions to enable estimation of the intrinsic rates of transformation. Intrinsic rates of transformation were obtained by combining a second order rate expression with an expression describing loss of transformation activity due to either endogenous decay or product toxicity. For HCFC-123 and HFC-134a, the independently measured endogenous decay rate for mixed culture MM1 (0.594/day) was sufficient to account for the observed loss of transformation activity with time. However, the endogenous decay rate did not account for the loss of transformation activity for HCFC-22 and HCFC-142b. A model based on product toxicity provided a reasonable representation of the loss of transformation activity for these compounds. The order of reactivity was HCFC-22〉HCFC-142b〉HFC-134a〉HCFC-123, with second order rate coefficients of 0.014, 0.0096, 0.00091, and 0.00054 l/mg-day, respectively. Transformation capacities for HCFC-22 and HCFC-142b were 2.47 and 1.11 µg substrate/mg biomass, respectively.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 21 (2000), S. 153-169 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Nebulette and nebulin are homologous proteins associated with the Z-lines of cardiac and skeletal muscle sarcomeres. Although these proteins share ∼70% sequence homology and an identical domain layout, nebulette is one-tenth the size of nebulin. To define structurally important features of these proteins in terms of the Z-line architecture, we have analyzed the primary structure of nebulette and nebulin from a variety of species and developmental stages. Alignment of the 35 residue nebulin-like modules from both proteins demonstrates that the individual modules share 30–90% homology across the six proteins analyzed. In addition, this analysis demonstrates a number of areas in which the identity across the six proteins is as high as 75%. These areas may be important signals for Z-line assembly and function in the striated muscles. Significantly, most of the areas of high identity also coincide with consensus phosphorylation sites. To evaluate if nebulette, like nebulin, exhibits tissue-specific and developmental specific polymorphism, a series of immunoblot assays were performed. These data demonstrate that nebulettes from different portions of the heart are the same size. Comparison of nebulette from embryonic and adult cardiac muscle also demonstrates that this protein does not appear to vary in size with developmental stage. Consistent with the large number of consensus phosphorylation sites identified in the nebulette primary structure, we find that nebulette is phosphorylated in the cardiac muscle at serine and threonine residues. These data and sequence analyses are discussed in terms of current models for Z-line architecture.
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  • 7
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Nebulin, a giant myofibrillar protein with size variants from 700 to 900 kDa in various skeletal muscles, has been proposed to constitute a set of inextensible filaments anchored at the Z-line and coextensive with actin filaments. To elucidate the architectural organization of this fourth set of myofilaments in the skeletal muscle sarcomere, we performed immunoelectron microscopic localization of epitope profiles of a number of site-specific monoclonal antibodies against cloned human nebulin fragments of known sequence loci. Monoclonal antibody N113, which is directed to fragment ND8 at approximately 300 residues away from the C-terminus, labelled the edges of Z-lines in both human quadriceps muscle and rabbit psoas muscle. Monoclonal antibody N101, which is directed to fragment NB5 near the N-terminal side, is localized to a single locus at 0.89 μm from the Z-line in human quadriceps muscle and 0.80μm from the Z-line in rabbit psoas muscle. Additionally, monoclonal antibody N109, which is directed to fragment NA3 on the carboxy side of the adjacent fragment NB5, is localized at 0.76 μm away from the Z-line in rabbit psoas muscle. This one-to-one correspondence between epitope loci and sequence loci demonstrates that a single nebulin polypeptide spans the length of the thin filament with its C-terminus anchored at the Z-line. The epitope spacings of site-specific antibodies are consistent with the notion that the nebulin filament is uniform in mass density along its length. We conclude that the thin filament, as defined morphologically by electron microscopy, is a composite filament of the conventional actin thin filament (actin/tropomyosin/troponin) and coextensible nebulin polypeptides which act as full-length molecular templates that regulate or stabilize colaterally the actin filament in the skeletal muscle sarcomere.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 56 (1997), S. 492-501 
    ISSN: 0006-3592
    Keywords: cometabolism ; methanotroph ; modeling ; trichloroethylene ; inhibition ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A model for cometabolism is verified experimentally for a defined methanotrophic mixed culture. The model includes the effects of cell growth, endogenous cell decay, product toxicity, and competitive inhibition with the assumption that cometabolic transformation rates are enhanced by reducing power obtained from oxidation of growth substrates. A theoretical transformation yield is used to quantify the enhancement resulting from growth substrate oxidation. A systematic method for evaluating model parameters independently is described. The applicability of the model is evaluated by comparing experimental data for methanotrophic cometabolism of TCE with model predictions from independently measured model parameters. Propagation of errors is used to quantify errors in parameter estimates and in the final prediction. The model successfully predicts TCE transformation and methane utilization for a wide range of concentrations of TCE (0.5 to 9 mg/L) and methane (0.05 to 6 mg/L). © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 56: 492-501, 1997.
    Additional Material: 7 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 205-225 
    ISSN: 0886-1544
    Keywords: myofibrillogenesis ; sarcomere structure ; Z-line ; protein ruler ; actin-binding protein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A 107-kD protein has been identified in primary cultures of chicken embryonic cardiomyocytes by immunoprecipitations with certain anti-nebulin monoclonal antibodies (mAbs). These mAbs, prepared against a fragment of human skeletal muscle nebulin located near the carboxyl terminus, detect a 107-kD protein in extracts of adult chicken heart, adult mouse heart, and adult rabbit heart by immunoblot analysis. A partial cDNA corresponding to this protein has been isolated by immunological screening of a chicken heart cDNA expression vector library. The partial cDNA encodes a 380-amino acid open reading frame composed entirely of nebulin-like 35-residue modules marked by the highly conserved sequence motifs: SXXXYK and TPD. The open reading frame exhibits 60-85% homology with skeletal muscle nebulins from a variety of species. This cDNA recognizes an ˜8-kb transcript in cardiac RNA and does not hybridize to skeletal muscle RNAs by northern analysis. Immunofluorescence localization of this nebulin-like protein in primary cultures of chicken cardiomyocytes and embryonic chicken cardiac myofibrils indicates that the protein is localized to the I-Z-I complex of the myofibrils, extending approximately 25% of the thin filament length. Comparisons of the distribution of this protein relative to actin, myosin, and titin in spreading cardiomyocytes suggest that the cardiac nebulin-like protein becomes aligned with the nascent myofibrils early during myofibrillogenesis. To distinguish this petite nebulin-like protein from the 600-900 kD skeletal muscle nebulin, we have named it nebulette. © 1995 Wiley-Liss, Inc.
    Additional Material: 10 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 24 (1993), S. 274-283 
    ISSN: 0886-1544
    Keywords: immunoelectron microscopy ; rabbit psoas ; elasticity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A “freeze-break” technique (Trombitás, K.: Acta Biochim. Biophys. Hung. 6:419-427, 1971) and immunoelectron microscopy were used to study the elastic properties of titin filaments. Small bundles of freshly prepared rabbit psoas muscle fibers were quickly frozen and broken under liquid nitrogen to fracture sarcomeres in planes perpendicular to the filament axis, in each of various regions along the sarcomere. The still-frozen specimens were thawed during fixation to allow elastic filaments to retract. The broken specimens were then labelled with monoclonal anti-titin antibodies against an unique epitope in the I-band.The titin epitopes were normally positioned symmetrically about the Z-line. However, in sarcomeres broken at the A-I junction, the epitopes no longer remained symmetrical: the titin filaments in the broken half-sarcomere retracted, independently of the thin filaments, forming a dense band just near the Z-line. The retracted density apparently did not reach the Z-line; retraction stopped at the level of the so-called N1-line. In sarcomeres broken at the Z-line level, the titin filaments retracted in the opposite direction. In this case the titin epitope retracted all the way to the ends of the thick filaments.It appears then that titin molecules form elastic filaments that are independent of thin filaments in most of the I-band. Near the Z-line, however, the titin filaments either have an inelastic domain or associate firmly with the thin filaments at the N1-line level. © 1993 Wiley-Liss, Inc.
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