LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 6 of total 6

Search options

  1. Article: Uroven' prolaktina v spinnomozgovoĭ zhidkosti i plazme krovi krupnogo rogatogo skota na raznykh étapakh ontogeneza.

    Taranenko, A A / Fedosimov, V A

    Fiziologicheskii zhurnal imeni I.M. Sechenova

    1994  Volume 80, Issue 10, Page(s) 32–38

    Abstract: The prolactine level in the CSF was shown to be higher than in the blood plasma in 5-8-month-old and 1-2-month-old calf. On the 9th month, the prolactine level in the blood becomes higher than in the CSF. No sexual difference was found in the prolactine ... ...

    Title translation The prolactin level in the cerebrospinal fluid and blood plasma of cattle at different stages of ontogeny.
    Abstract The prolactine level in the CSF was shown to be higher than in the blood plasma in 5-8-month-old and 1-2-month-old calf. On the 9th month, the prolactine level in the blood becomes higher than in the CSF. No sexual difference was found in the prolactine levels. The data obtained suggest an extrahypophyseal origin of the CSF prolactine and its important role in early stages of the ontogeny.
    MeSH term(s) Aging/metabolism ; Animals ; Cattle/metabolism ; Female ; Fetus/metabolism ; Male ; Prolactin/analysis ; Prolactin/metabolism ; Radioimmunoassay
    Chemical Substances Prolactin (9002-62-4)
    Language Russian
    Publishing date 1994-10
    Publishing country Russia (Federation)
    Document type Comparative Study ; English Abstract ; Journal Article
    ZDB-ID 33354-2
    ISSN 1027-3646 ; 0015-329X ; 0869-8139
    ISSN 1027-3646 ; 0015-329X ; 0869-8139
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article: Dvu tipa prolaktinsviazyvaiushchikh mest na membranakh zhirovykh golbulmoloka korov.

    Larina, M M / Fedosimov, V A

    Biokhimiia (Moscow, Russia)

    1992  Volume 57, Issue 6, Page(s) 838–844

    Abstract: Prolactin (PRL) binding to specific receptors of cow milk fat globular membranes (MFGM) has been studied. The data obtained point to the existence of two PRL-binding sites on cow MFGM. The parameters of PRL binding to lactogenic receptors have been ... ...

    Title translation Two types of prolactin-binding sites on membranes of cow milk fat globules.
    Abstract Prolactin (PRL) binding to specific receptors of cow milk fat globular membranes (MFGM) has been studied. The data obtained point to the existence of two PRL-binding sites on cow MFGM. The parameters of PRL binding to lactogenic receptors have been estimated for a two-binding-site model.
    MeSH term(s) Animals ; Binding Sites ; Cattle ; Membrane Glycoproteins/metabolism ; Milk/metabolism ; Mucin-1 ; Prolactin/metabolism
    Chemical Substances Membrane Glycoproteins ; Mucin-1 ; Prolactin (9002-62-4)
    Language Russian
    Publishing date 1992-06
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article
    ZDB-ID 1109-5
    ISSN 1608-3040 ; 0320-9725 ; 0006-2979 ; 0320-9717
    ISSN (online) 1608-3040
    ISSN 0320-9725 ; 0006-2979 ; 0320-9717
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  3. Article: Gidroliz prolaktina serinovoĭ proteinazoĭ mitokhondriĭ sekretornykh kletok molochnoĭ zhelezy.

    Khropycheva, R P / Marinchenko, G V / Fedosimov, V A

    Biokhimiia (Moscow, Russia)

    1992  Volume 57, Issue 6, Page(s) 945–955

    Abstract: Mitochondrial proteinase isolated from secretory cells of the mammary gland of lactating rats able to hydrolyze 125I-labeled and native prolactin (PRL) has been studied. The enzyme represents a serine proteinase and is localized in the inner ... ...

    Title translation Hydrolysis of prolactin by a serine proteinase from mammary gland secretory cell mitochondria.
    Abstract Mitochondrial proteinase isolated from secretory cells of the mammary gland of lactating rats able to hydrolyze 125I-labeled and native prolactin (PRL) has been studied. The enzyme represents a serine proteinase and is localized in the inner mitochondrial membrane. The molecular mass of the enzyme is 17-18 kDa, pH optimum is at 8.0-9.0. Partial purification of the enzyme has been carried out. The Km constant for 125I-PRL is equal to 10(-6) M, that for 2% hemoglobin is 1.2 x 10(-4) M. Analysis of products of rat and ovine PRL hydrolysis by proteinase using high performance liquid chromatography and PAAG electrophoresis revealed the formation of large-size fragments of the hormone. A possible role of proteinase in the mechanism of PRL action on mammary gland tissues is discussed.
    MeSH term(s) Animals ; Chromatography, High Pressure Liquid ; Chromatography, Liquid ; Electrophoresis, Polyacrylamide Gel ; Hydrolysis ; Intracellular Membranes/enzymology ; Iodine Radioisotopes ; Lactation ; Mammary Glands, Animal/enzymology ; Mitochondria/enzymology ; Prolactin/metabolism ; Rats ; Rats, Wistar ; Serine Endopeptidases/metabolism
    Chemical Substances Iodine Radioisotopes ; Prolactin (9002-62-4) ; Serine Endopeptidases (EC 3.4.21.-)
    Language Russian
    Publishing date 1992-06
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article
    ZDB-ID 1109-5
    ISSN 1608-3040 ; 0320-9725 ; 0006-2979 ; 0320-9717
    ISSN (online) 1608-3040
    ISSN 0320-9725 ; 0006-2979 ; 0320-9717
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  4. Article: Laktogennye retseptory na kletkakh granulezy korov.

    Lebedeva, I Iu / Lebedev, V A / Fedosimov, V A / Kuz'mina, T I

    Biokhimiia (Moscow, Russia)

    1994  Volume 59, Issue 7, Page(s) 1062–1066

    Abstract: Bovine prolactin (BPRL) binding to cow granulosa cells depending on the antral follicular diameter has been studied. The data obtained point to the existence of one type of low affinity PRL-binding sites on granulosa cells. No reliable differences in the ...

    Title translation Lactogenic receptors on cow granulosa cells.
    Abstract Bovine prolactin (BPRL) binding to cow granulosa cells depending on the antral follicular diameter has been studied. The data obtained point to the existence of one type of low affinity PRL-binding sites on granulosa cells. No reliable differences in the parameters of BPRL interaction with lactogenic receptors in the dynamics of folliculogenesis have been found. The recombinant bovine growth hormone and BPRL competitive binding while interacting with lactogenic receptors has been shown that suggests action of these hormones at over the same binding sites on cow granulosa cells.
    MeSH term(s) Animals ; Binding Sites ; Cattle ; Female ; Granulosa Cells/metabolism ; Growth Hormone/metabolism ; Receptors, Prolactin/metabolism ; Recombinant Proteins/metabolism
    Chemical Substances Receptors, Prolactin ; Recombinant Proteins ; Growth Hormone (9002-72-6)
    Language Russian
    Publishing date 1994-07
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article
    ZDB-ID 1109-5
    ISSN 1608-3040 ; 0320-9725 ; 0006-2979 ; 0320-9717
    ISSN (online) 1608-3040
    ISSN 0320-9725 ; 0006-2979 ; 0320-9717
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  5. Article: Issledovanie urovnia prolaktina v krovi zhvachnykh zhivotnykh

    Taranenko, A G / Kasimov, Z N / Fedosimov, V A

    Fiziologicheskii zhurnal SSSR imeni I. M. Sechenova

    1975  Volume 61, Issue 4, Page(s) 648–654

    Abstract: The contents of prolactin in the blood of male ruminants and dry-period, pregnant, and lactating female ruminants was studied by a radioimmunological method. The prolactin was found to take part not only in the lactation processes but in some other ... ...

    Title translation Prolactin levels in the blood of ruminants.
    Abstract The contents of prolactin in the blood of male ruminants and dry-period, pregnant, and lactating female ruminants was studied by a radioimmunological method. The prolactin was found to take part not only in the lactation processes but in some other functions too. The utmost changes of the prolactin contents were observed during milking: the release of prolactin from the adenohypophysis is the unconditioned reflex action. The conditioning of the hormone release into the blood is also possible. Nociceptive stimulation or adrenalin administration reduce the level of the hormone. The hand milking is more adequate as compared with the machine one and results in the higher level of prolactin in the blood. The character of the prolactin contents changes in the blood makes it possible to recommend this parameter for a physiological estimation of milking apparata.
    MeSH term(s) Animals ; Cattle/blood ; Female ; Goats/blood ; Lactation ; Male ; Pregnancy ; Pregnancy, Animal ; Prolactin/blood
    Chemical Substances Prolactin (9002-62-4)
    Language Russian
    Publishing date 1975-04
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article
    ZDB-ID 219224-x
    ISSN 0015-329X
    ISSN 0015-329X
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  6. Article: A study of the ruminants' blood prolactin level

    Taranenko, A.H / Kasimov, Z.N / Fedosimov, V.A

    Apr 1975, 61 (4)

    1975  

    Keywords zoology ; livestock ; animal science
    Language Russian
    Dates of publication 1975-04
    Size p. 648-654.
    Document type Article
    Note In Russian; Includes summary in English ; Title in original language could not be transcribed.
    Database NAL-Catalogue (AGRICOLA)

    Kategorien

To top