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  • 1
    Electronic Resource
    Electronic Resource
    Superconducting, electronic and magnetic anomalies due to structural transition around x=0.12 in La"2"-"xBa"xCuO"4
    Amsterdam : Elsevier
    Physica C: Superconductivity and its applications 185-189 (1991), S. 913-914 
    Details
    ISSN: 0921-4534
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0921-4534(91)91680-3
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Myosin light chain patterns in histochemically typed single fibers of the rat skeletal muscle
    Amsterdam : Elsevier
    Comparative Biochemistry and Physiology -- Part B: Biochemistry and 102 (1992), S. 617-620 
    Details
    ISSN: 0305-0491
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0305-0491(92)90056-W
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  • 3
    Electronic Resource
    Electronic Resource
    Changes in myosin heavy chain isoform expression of overloaded rat skeletal muscles
    Amsterdam : Elsevier
    International Journal of Biochemistry 25 (1993), S. 1609-1613 
    Details
    ISSN: 0020-711X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0020-711X(93)90519-K
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  • 4
    Electronic Resource
    Electronic Resource
    Identification of fiber types in rat skeletal muscle based on the sensitivity of myofibrillar actomyosin ATPase to copper (1984)
    Springer
    Histochemistry and cell biology 81 (1984), S. 379-383 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Experiments are reported demonstrating that differential rates of inactivation of the histochemical staining for myofibrillar actomyosin ATPase in rat skeletal muscle fibers exist following inclusion of low concentrations of Cu2+ in the preincubation medium. This response of rat muscle occurs at near neutral (7.40), acid (4.60), and alkaline (10.30) pH. The response to Cu2+ appears to result from a binding of Cu2+ onto the myofibrillar complex, probably on myosin itself, as it can be reversed by soaking of the pretreated muscle sections in sodium cyanide or the Cu2+ chelator diethyldithiocarbamate. The pattern of modification of the staining pattern following pretreatment with Cu2+ is the mirror image of that produced by pretreatment with acid. The results demonstrate that the inclusion of Cu2+ in the preincubation media for the myofibrillar actomyosin ATPase can be a useful tool to differentiate fiber types. They also support the earlier conclusion that three distinct types of type II fibers can be identified in rat skeletal muscle based on the histochemical staining for myofibrillar actomyosin ATPase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00514333
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  • 5
    Electronic Resource
    Electronic Resource
    Comparison of fiber types in skeletal muscles from ten animal species based on sensitivity of the myofibrillar actomyosin ATPase to acid or copper (1985)
    Springer
    Histochemistry and cell biology 82 (1985), S. 175-183 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Comparisons were made of the histochemical characteristics of skeletal muscle from 10 animal species. The basic comparison was made from the staining patterns for the myofibrillar actomyosin ATPase produced by preincubation of fresh frozen cross-sections of muscle at alkaline pH (10.30) or acid pH (4.60) with those produced by preincubation in media containing Cu2+ at alkaline pH (10.30), near neutral pH (7.40), or acid pH (4.60). Muscle sections were also stained for reduced nicotinamide adenine dinucleotide tetrazolium reductase and alpha-glycerophosphate dehydrogenase to provide an indication of the relative oxidative and glycolytic capacity of the different fiber types. Type II fibers in mixed fibered muscles were either very sensitive, moderately sensitive, or relatively insensitive to inactivation of the myofibrillar actomyosin ATPase after acid preincubation. These fibers were identified as type IIA1, IIA2, and IIA3, respectively. The myofibrillar actomyosin ATPase of the type I fibers of these muscles, with the exception of those in mouse muscle, was activated by pretreatment with acid. A separation of animal species was possible based on the stability of the IIA1 fibers to inclusion of Cu2+ in the preincubation medium. For one group of animals (rat, mouse, monkey, man, dog, rabbit, and cow), a reciprocal relationship existed between lability to acid and stability to Cu2+ for type IIA1 and IIA3 fibers, respectively. For the second group of animals (horse, ass, and cat) there was a parallel relationship between lability or stability of the type IIA1 and IIA3 fibers to pretreatment with either acid or Cu2+
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00708203
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  • 6
    Electronic Resource
    Electronic Resource
    Influence of ionic composition, buffering agent, and pH on the histochemical demonstration of myofibrillar actomyosin ATPase (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 609-614 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The influence of the composition of the preincubation medium on the histochemical demonstration of myofibrillar actomyosin ATPase, including a variety of carboxylic acid and non-carboxylic acid buffering compounds and neutral salts, was studied. In inorganic salt-free systems the rate of the activation of type I fibers and inactivation of type II fibers was accelerated when the carboxylic acids had longer chain length or multiple carobxyl groups. Of these factors, the number of carboxyl groups was dominant with a 100 mM citrate buffer producing a sharp differentiation between fiber types. In contrast, the time course of the response was exceptionally long in an acetate buffer. The time course of the ATPase reaction was also modified by other buffers at pH 4.60. The most notable were an ascorbate — glycine buffer system which produced little or no deviation from the alkaline preincubation staining pattern after prolonged preincubation and a pyrophosphate system which produced a rapid change. Neutral salts in the preincubation medium accelerated the time course of the inactivation — activation process with the order for the halogen salts of K+ being F−〈Cl−〈Br−〈I−, which is a progression by molecular weight. The only sequence for cations on the myofibrillar actomyosin ATPase was Li+〈 Na+〈K+. The response to salts was concentration dependent. An interaction existed between buffering compound, type of salt, and pH. These experiments demonstrate that the histochemical differentiation of fiber types by the myofibrillar actomyosin ATPase reaction depends upon a modification of some component(s) of the myofibrillar complex that can be influenced by a number of factors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553725
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  • 7
    Electronic Resource
    Electronic Resource
    Influence of exercise on the fiber composition of skeletal muscle (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 553-557 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Biopsy samples from the vastus lateralis muscle (VLM) of man were examined for fiber composition at rest and at selected intervals during prolonged exercise ranging in intensity from 40% to 75% of the total body maximal oxygen uptake (VO 2max) and one-min bouts of exercise at 150%VO 2max. Because of the heterogeneity of fibers in human VLM, studies were also completed where the effect of exercise on the fiber composition of the rat soleus muscle (SM) was examined. In some animals the SM from one hindlimb was removed 9 days prior to their being exercised after which the remaining SM was removed. Exercise reduced muscle glycogen in all experiments. In the studies with man, blood lactate exceeded 17 mmoles/l after the heavy exercise but was largely unchanged by endurance exercise. Colonic temperature of the exercised rats exceeded 40° C. In studies where fibers were identified only as type I and type II, type II fibers in the VLM of all samples (16) taken at rest averaged 61.2±12.5% as compared to 59.0±12.0% after exercise (54 biopsy samples). In a second series of studies with man where the subtypes of type II fibers were identified, there were also no differences in fiber composition of the VLM after varying periods of exercise. Glycogen content and percent fiber composition were the same in right and left SM obtained from rested rats. Exercise (30 to 40 min) did not alter the fiber composition of the rat SM. These data demonstrate that the histochemically demonstratable myofibrillar actomyosin ATPase of skeletal muscle is not altered by a single exercise bout.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02400971
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  • 8
    Electronic Resource
    Electronic Resource
    Influence of exercise on the fiber composition of skeletal muscle (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 553-557 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Biopsy samples from the vastus lateralis muscle (VLM) of man were examined for fiber composition at rest and at selected intervals during prolonged exercise ranging in intensity from 40% to 75% of the total body maximal oxygen uptake (VO 2max) and one-min bouts of exercise at 150%VO 2max. Because of the heterogeneity of fibers in human VLM, studies were also completed where the effect of exercise on the fiber composition of the rat soleus muscle (SM) was examined. In some animals the SM from one hindlimb was removed 9 days prior to their being exercised after which the remaining SM was removed. Exercise reduced muscle glycogen in all experiments. In the studies with man, blood lactate exceeded 17 mmoles/l after the heavy exercise but was largely unchanged by endurance exercise. Colonic temperature of the exercised rats exceeded 40° C. In studies where fibers were identified only as type I and type II, type II fibers in the VLM of all samples (16) taken at rest averaged 61.2±12.5% as compared to 59.0±12.0% after exercise (54 biopsy samples). In a second series of studies with man where the subtypes of type II fibers were identified, there were also no differences in fiber composition of the VLM after varying periods of exercise. Glycogen content and percent fiber composition were the same in right and left SM obtained from rested rats. Exercise (30 to 40 min) did not alter the fiber composition of the rat SM. These data demonstrate that the histochemically demonstratable myofibrillar actomyosin ATPase of skeletal muscle is not altered by a single exercise bout.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553716
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  • 9
    Electronic Resource
    Electronic Resource
    Influence of ionic composition, buffering agent, and pH on the histochemical demonstration of myofibrillar actomyosin ATPase (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 609-614 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The influence of the composition of the preincubation medium on the histochemical demonstration of myofibrillar actomyosin ATPase, including a variety of carboxylic acid and non-carboxylic acid buffering compounds and neutral salts, was studied. In inorganic salt-free systems the rate of the activation of type I fibers and inactivation of type II fibers was accelerated when the carboxylic acids had longer chain length or multiple carobxyl groups. Of these factors, the number of carboxyl groups was dominant with a 100 mM citrate buffer producing a sharp differentiation between fiber types. In contrast, the time course of the response was exceptionally long in an acetate buffer. The time course of the ATPase reaction was also modified by other buffers at pH 4.60. The most notable were an ascorbate — glycine buffer system which produced little or no deviation from the alkaline preincubation staining pattern after prolonged preincubation and a pyrophosphate system which produced a rapid change. Neutral salts in the preincubation medium accelerated the time course of the inactivation — activation process with the order for the halogen salts of K+ being F−〈Cl−〈Br−〈I−, which is a progression by molecular weight. The only sequence for cations on the myofibrillar actomyosin ATPase was Li+〈 Na+〈K+. The response to salts was concentration dependent. An interaction existed between buffering compound, type of salt, and pH. These experiments demonstrate that the histochemical differentiation of fiber types by the myofibrillar actomyosin ATPase reaction depends upon a modification of some component(s) of the myofibrillar complex that can be influenced by a number of factors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02400980
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  • 10
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    Effect of pressure on the magnetoresistance of magnetic multilayers with two magnetic components (1997)
    Elsevier
    Details
    Publication Date: 1997-07-01
    Print ISSN: 0921-4526
    Electronic ISSN: 1873-2135
    Topics: Physics
    Published by Elsevier
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