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  • 1
    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
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 32 (1967), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SUMMARY— Post-mortem changes in nucleoside triphosphatase activity of bovine myosin B have been studied by using several different modifiers with either 5 mM ATP or 5 mM ITP as substrate at ionic strengths (r/2) of 0.09, 0.19, or 0.52. Enzymic activity was determined by measuring the release of inorganic phosphate. There was very little difference in enzymic activity between myosin B isolated from prerigor, rigor (24 hr post-mortem) or post-rigor (312 hr post-mortem) muscle stored at either 2° or 16°C except that the specific activity of myosin B prepared from muscle stored for 12–24, hr post-mortem was higher than activity of myosin B prepared immediately after death. This increase cannot be explained in terms of rigor shortening, but suggests that a change in myosin conformation or in the nature of the actin-myosin interaction occurs in post-mortem muscle. If an actin-myosin interaction occurs during rigor mortis and if this association remains unchanged during extraction of myosin B, then the very low Mg++-modified myosin B enzymic activities obtained at Γ/2 = 0.19 and 0.52 indicate that this interaction is not irreversible. Extraction in the absence of ATP produced a myosin B whose ATPase activity was markedly inhibited by trace amounts of Mg++. This may be due to the absence of a-actinin in these myosin B preparations. No consistent differences in activation energies were found either at Γ/2 = 0.19 or 0.52 among the NTPase reactions of myosin B samples prepared from muscle after various times of post-mortem storage.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Evidence suggests that desmin, titin and nebulin, three recently discovered proteins, have cytoskeletal roles in muscle cells. The three proteins have been purified from mature skeletal muscle and partially characterized. Properties of the three proteins are described, with special regard to their probable roles and importance in maintaining muscle cell integrity. Results will be shown that demonstrate ability of purified desmin to self-assemble into synthetic 10-nm (intermediate) diameter filaments. Taken together with immunoelectron microscope results (Richardson et al. 1981), it is evident that desmin is the major component of 10-nm filaments of mature skeletal muscle cells and that the desmin filaments link adjacent myofibrils at their Z-line levels and seemingly tie the myofibrils into the cell cyto-skeleton. Desmin is degraded at about the same rate as is the highly susceptible troponin-T in bovine semitendinosus muscle postmortem. Alterations in desmin and other recently discovered cytoskeletal proteins would be expected to disrupt muscle cell integrity and to have marked effects on properties of muscle important to its use as food.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 51 (1986), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Purified cathepsin D was incubated with bovine skeletal muscle myofibrils under in virro conditions resembling those found in postmortem muscle. SDS-PAGE analysis of myofibrils treated at pH 5.5 and 37°C and the sedimented, showed degradation of myosin heavy chains and titin. A small amount of actin, tropomyosin, troponins T and I, and myosin light chains also were degraded. The cathepsin D treated myofibrils were not fragmented to any greater extend than untreated myofibrils. Raising the pH and/or lowering the temperature greatly reduced the effectiveness of cathepsin D suggesting that the enzyme does not play a principal role in the tenderization process occurring in muscle postmortem.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This study examined the in vitro effects of calcium-activated protease (CAF) on bovine myofibrillar proteins and structure under postmortem-like conditions of pH and temperature. Effects usually associated with this enzyme under optimal conditions were reduced as temperature and/or pH were lowered. However, significant activity remained at 15°C and pH 6.5, and some activity was detectable at even lower pH's and temperatures. Effects observed included: solubilization of myofibrillar protein, degradation of the myofibrillar protein titin and others, and an increase in the degree of myofibrillar fragmentation. These results suggest that CAF is able to hydrolyze proteins that are important to structural integrity under conditions mimicking those present in postmortem muscle.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 455 (1985), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 271 (1978), S. 265-267 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Skeletal muscle containing nemaline rods was obtained by biopsy from a patient with congenital rod disease (second biopsy, case No. 1; see ref. 20 for clinical details) and stored at - 60 C until glycerination. It has been shown previously that glyceration does not alter fine structure of the ...
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-119X
    Keywords: Cytoskeleton Desmin knock-out mice Intermediate filament-associated proteins Myotendinous junctions Neuromuscular junctions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Mice lacking the gene encoding for the intermediate filament protein desmin have a surprisingly normal myofibrillar organization in skeletal muscle fibers, although myopathy develops in highly used muscles. In the present study we examined how synemin, paranemin, and plectin, three key cytoskeletal proteins related to desmin, are organized in normal and desmin knock-out (K/O) mice. We show that in wild-type mice, synemin, paranemin, and plectin were colocalized with desmin in Z-disc-associated striations and at the sarcolemma. All three proteins were also present at the myotendinous junctions and in the postsynaptic area of motor endplates. In the desmin K/O mice the distribution of plectin was unaffected, whereas synemin and paranemin were partly affected. The Z-disc-associated striations were in general no longer present in between the myofibrils. In contrast, at the myotendinous and neuromuscular junctions synemin and paranemin were still present. Our study shows that plectin differs from synemin and paranemin in its binding properties to the myofibrillar Z-discs and that the cytoskeleton in junctional areas is particularly complex in its organization.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 0886-1544
    Keywords: intermediate filaments ; cytoskeleton ; filament attachment sites ; immunogold labeling ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The substructure of assembling cytoplasmic dense bodies (CDBs) and changes in the distribution of desmin and α-actinin during development of smooth muscle were studied in gizzard samples from 10- and 16-day embryos and from 1- and 7-day post-hatch chickens. CDBs in these cells lack the density of CDBs in mature or adult smooth muscle cells and, thus, allow observations of the changes inside CDBs. The random filament orientation seen in younger embryonic cells is first modified to include relatively small patches of IFs that are somewhat straighter and are approaching a side-by-side arrangement. As development proceeds, the IFs in these arrays become straighter, are parallel over longer lengths of the IFs and later acquire the density characteristic of mature CDBs. Anti-desmin labeling in embryonic 10- and 16-day cells showed that desmin intermediate filaments (IFs) were located in the myofilament compartment but were concentrated in or near assembling CDBs. Anti-desmin labeling shifted to the perimeter of CDBs after hatching. Cross sections, longitudinal sections, and stereo pairs all show that IF profiles are present inside unlabeled assembling CDBs. Anti-α-actinin labeling was directly on CDBs and was often associated with the cross-connecting filaments (CCFs) (average diameter of 2-3nm) inside CDBs. We propose, based on these data, that desmin IFs, α-actinin-containing CCFs, and actin filaments are the principal components of the substructure of assembling CDBs. We also present a proposed model for CDB assembly. © 1994 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Rat soleus muscle Z-lines and Z-line anomalies induced by neostigmine methyl sulfate (NMS) and cat soleus muscle Z-line and Z-line anomalies induced by tentomy were examined by electron microscopy before and after dissection of muscle fibers with Ca2+-activated neutral protease (CAF) to elucidate structural properties of Z-lines and related Z-line-type structures. In both normal and treated muscles, interdigitation of thin (6-7 nm) filaments, which were continuous with I-filaments (actin) from adjacent sarcomeres, was observed at the Z-line in longitudinal section.Both neostigmine methyl sulfate and tenotomy treatments induced muscle atrophy associated with Z-line degradation, streaming, and irregular distribution and accumulation of Z-line material and Z-rod formation. Tenotomized muscle also was characterized by the presence of N-line-like bands and I-Z-I brushes. CAF digestion removed the electron-dense covering material from Z-rods and revealed a backbone of actin filaments. The origin of Z-rods, their structural similarity to Z-lines in longitudinal and cross section, and their susceptibility to CAF indicate that Z-rods are directly related to native Z-lines and are probably lateral polymers of a basic Z-line unit.The regular square net alignment (22 nm) of I-filaments (actin) in cross sections of I-Z-I brushes which contain no N-lines suggests that the I-square net arrangement near the Z-line is determined by Z-filament-actin filament interaction rather than by the N-line or other factors.The results suggest that I-filaments (actin) penetrate the mammalian Z-line and are Z-line constituents and that the width of Z-lines and the length of Z-rods are determined by the amount of overlap of actin filaments. The perpendicular periodicity of Z-rods and the zigzag-oblique arrowheadlike appearance seen in longitudinal section of Z-lines are attributed to α-actinin.
    Additional Material: 27 Ill.
    Type of Medium: Electronic Resource
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