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  • 1955-1959  (4)
  • 1
    Electronic Resource
    Electronic Resource
    The action of x-rays on the motor function and the contractile proteins of motile cells (1959)
    Springer
    Bulletin of experimental biology and medicine 48 (1959), S. 1483-1486 
    Details
    ISSN: 1573-8221
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Experiments showed that there are no significant changes of the motor function in the seminal cells after x-ray irradiation of frogs (20, 000 r). This shows that disturbance of oxidative phosphorylation under the action of radiation is not a general biological regularity. The effect of ionizing radiation on the resynthesis of highenergy (ATP) differs in the cells of radiosensitive and radioresistant tissues; evidently it is primarily determined by the different localization of the corresponding enzyme systems therein. There are no visible disturbances in the ability of “glycerol models” of myofibrils, the cilia of the ciliated epithelium and spermatozoa (obtained from the tissues of irradiated animals), to interact with ATP. This points to a rather low radiosensitivity of the contractile cellular proteins and explains the high radioresistance in some phases of cell division connected with the separation of the chromosomes and equatorial division of the cytoplasm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00792740
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The action of a high pressure on the adenosinetriphatase activity of myosin (1959)
    Springer
    Bulletin of experimental biology and medicine 47 (1959), S. 690-692 
    Details
    ISSN: 1573-8221
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Solutions of reprecipitated myosin lose completely their adenosinetriphosphates activity under the effect of high pressure (4000 atmospheres). However, they retain their ability to readily dissolve in 0.6 M KCl and to become precipitated in subsequent dialysis or after considerable dilution of myosin salt solution with water. The viscosity of myosin, free of actomyosin admixture, rises under the effect of high pressure. Myosin subjected to the effect of high pressure loses its ability to combine with an activated actin with the formation of actomyosin. The viscosity of actomyosin gels subject to high pressure (4000 atmospheres) does not diminish after addition of adenosinetriphosphates. Under the effect of high pressure there must occur some kinds of changes in the myosin structure, these being associated with inactivation of certain groups (possibly SH) and imparting to myosin an enzymatic character without, however, making it lose its hydrophilic properties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00781221
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The actin content of the myometrium (1959)
    Springer
    Bulletin of experimental biology and medicine 48 (1959), S. 1110-1113 
    Details
    ISSN: 1573-8221
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Proteins extracted by Weber's solution from the smooth muscle of the uterus do not possess the ability to interact with myosin preparations with the formation of actomyosin. This makes highly improbable the assumption of Snellman and Tenow on the presence of any appreciable amounts of free actin in 0.5 M KCL extracts of myometrium. Investigations conducted by the method of paper electrophoresis demonstrate the presence of 3 fractions in the myometrium extracts with high ionic potential, viz., myoalbumin, heterogeneous myogen and actomyosin. The latter consists of a small quantity of actomyosin (undoubtedly bound with nucleoproteins) and water-soluble myofibrillar proteins (mainly tropomyosin and possibly Δ-protein). Likewise these investigations give no grounds for associating the peculiarity of the myometrial proteins with the high concentration of the “easily extractable” actin in the muscles of the uterus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00868911
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The existence of globulin X as an individual protein (1959)
    Springer
    Bulletin of experimental biology and medicine 48 (1959), S. 838-841 
    Details
    ISSN: 1573-8221
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The quantitative content of globulin X was investigated in the muscle juice obtained by pressing the striped muscles of embryos, newborn and adult rabbits. The globulin X percentage was also determined in various fractions of the muscle juice salted out with ammonium sulfate. Electrophoretic investigation of water-insoluble muscle globulins was also conducted. The data obtained led the authors to a conclusion that globulin is not an individual protein but a mixture of different globulins varying according to their physicochemical properties. Electrophoretically, globulin is not detected as a separate component. Its content in the striped muscle juice changes during the process of ontogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00788196
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    Paper (German National Licenses)
    Fulltext
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