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  • Proceedings of the National Academy of Sciences  (34)
  • 1975-1979  (34)
  • Natural Sciences  (34)
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  • Proceedings of the National Academy of Sciences  (34)
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Language
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  • 1975-1979  (34)
Year
FID
Subjects(RVK)
RVK
  • 1
    Online Resource
    Online Resource
    Human somatotropin: biological characterization of the recombinant molecule.
    Proceedings of the National Academy of Sciences ; 1976
    In:  Proceedings of the National Academy of Sciences Vol. 73, No. 10 ( 1976-10), p. 3463-3465
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 73, No. 10 ( 1976-10), p. 3463-3465
    Abstract: The recombinant hormone obtained by non-covalent interaction of the NH2-terminal 134 amino acid fragment with the COOH-terminal 51 amino acid fragment of the reduced-carbamidomethylated human somatotropin molecule is found to exhibit nearly full biological activity of the native hormone, as evidenced by the stimulation of hepatic ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) in vivo and protein synthesis in mouse mammary gland in vitro. Radioimmunoassay data indicate that the recombinant behaves immunochemically in a manner almost identical to that of the native hormone.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.73.10.3463
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1976
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 2
    Online Resource
    Online Resource
    Isolation and structure of an untriakontapeptide with opiate activity from camel pituitary glands.
    Proceedings of the National Academy of Sciences ; 1976
    In:  Proceedings of the National Academy of Sciences Vol. 73, No. 4 ( 1976-04), p. 1145-1148
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 73, No. 4 ( 1976-04), p. 1145-1148
    Abstract: The isolation of an untriakontapeptide from camel pituitary extracts has been described. Its structure has been determined and shown to be identical to the sequence of carboxyl-terminal 31 amino acids of ovine beta-lipotropin. The peptide possesses very low lipotropic activity but significant opiate activity.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.73.4.1145
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1976
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 3
    Online Resource
    Online Resource
    Maintenance of genetic variability under mutation and selection pressures in a finite population.
    Proceedings of the National Academy of Sciences ; 1977
    In:  Proceedings of the National Academy of Sciences Vol. 74, No. 6 ( 1977-06), p. 2509-2513
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 74, No. 6 ( 1977-06), p. 2509-2513
    Abstract: Formulas are developed for the distribution of allele frequencies and the mean and variance of heterozygosity under mutation and selection pressures. In large populations, even slight selection drastically changes the shape of the distribution of allele frequencies and reduces heterozygosity. On the other hand, the number of rare alleles in a sample is much less affected by selection. Under genic selection, heterozygosity may decrease with increasing population size. As a test statistic, the variance of heterozygosity can be used to detect the presence of selection, though it is not efficient when selection is very slight.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.74.6.2509
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1977
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 4
    Online Resource
    Online Resource
    beta-endorphin is a potent analgesic agent.
    Proceedings of the National Academy of Sciences ; 1976
    In:  Proceedings of the National Academy of Sciences Vol. 73, No. 8 ( 1976-08), p. 2895-2898
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 73, No. 8 ( 1976-08), p. 2895-2898
    Abstract: beta-Endorphin, an opiate-like peptide, has potent antinociceptive properties when it is administered directly into the brain and assayed in the the tail-flick, hot-plate, and writhing tests in mice and in the wet shake test in rats. On a molar basis, beta-endorphin is 18 to 33 times more potent than morphine and its actions are blocked by the specific opiate antagonist, naloxone hydrochloride. The activity of beta-endorphin in vivo is also compared to other peptides that show opiate-like activity in assays in vitro.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.73.8.2895
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1976
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 5
    Online Resource
    Online Resource
    Structure and properties of a hybrid tryptophan synthetase of alpha chain produced by genetic exchange between Escherichia coli and Salmonella typhimurium.
    Proceedings of the National Academy of Sciences ; 1977
    In:  Proceedings of the National Academy of Sciences Vol. 74, No. 1 ( 1977-01), p. 286-290
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 74, No. 1 ( 1977-01), p. 286-290
    Abstract: Genetic exchange between the structural genes for the alpha chain of tryptophan synthetase [tryptophan synthase; L-serine hydro-lyase (adding indoleglycerol-phosphate), EC 4.2.1.20] of E. coli and S. typhimurium yielded recombinant genes that specified functional hybrid polypeptides. The alpha chains produced by three recombinants appeared to be identical but differed from those of E. coli and S. typhimurium by at least 27 and 8 amino acid residues, respectively. In vivo and in vitro tests of enzyme function suggest that the hybrid alpha chains are near-equivalent to their fully active parental proteins.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.74.1.286
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1977
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 6
    Online Resource
    Online Resource
    Human pituitary growth hormone: a biologically active hendekakaihekaton peptide fragment corresponding to amino-acid residues 15-125 in the hormone molecule.
    Proceedings of the National Academy of Sciences ; 1975
    In:  Proceedings of the National Academy of Sciences Vol. 72, No. 10 ( 1975-10), p. 3878-3882
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 72, No. 10 ( 1975-10), p. 3878-3882
    Abstract: A hendekakaihekaton peptide fragment has been prepared by cyanogen bromide cleavage of the NH2-terminal 134-residue fragment of human pituitary growth hormone. It was characterized by amino-acid and end-group analyses, exclusion chromatography, disc electrophoresis, circular dichroism, and ultracentrifugation. The fragment, corresponding to amino-acid residues 15-125 in the hormone molecule, possesses hepatic ornithine decarboxylase (EC 4.1.1.17; L-ornithine carboxy-lyase) stimulating, lactogenic, and somatotrophic activity. It has immunoreactivity in the microcomplement-fixation and radioimmunoassay experiments. The circular dichroism data indicate that the hendekakaihekaton peptide fragment is devoid of secondary and tertiary structure.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.72.10.3878
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1975
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 7
    Online Resource
    Online Resource
    beta-Endorphin: cross tolerance to and cross physical dependence on morphine.
    Proceedings of the National Academy of Sciences ; 1976
    In:  Proceedings of the National Academy of Sciences Vol. 73, No. 11 ( 1976-11), p. 4187-4189
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 73, No. 11 ( 1976-11), p. 4187-4189
    Abstract: The effects of beta-endorphin on the antinociceptive responses and abrupt withdrawal jumping in morphine-dependent mice were studied. Mice were rendered morphine dependent by implantation of a morphine pellet (75 mg base) for 3 days. The analgesic response to beta-endorphin decreased after morphine pellet implantation, as evidenced by an eight-fold increase in the median antinociceptive dose of morphine was found. In small doses (0.09-0.17 mug per mouse), beta-endorphin suppressed abrupt withdrawal jumping. Met-enkephalin, even in high doses (200 mug per mouse), did not suppress abrupt withdrawal jumping.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.73.11.4187
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1976
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 8
    Online Resource
    Online Resource
    beta-Endorphin: synthesis of analogs modified at the carboxyl terminus with increased activites.
    Proceedings of the National Academy of Sciences ; 1979
    In:  Proceedings of the National Academy of Sciences Vol. 76, No. 7 ( 1979-07), p. 3276-3278
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 76, No. 7 ( 1979-07), p. 3276-3278
    Abstract: Three analogs of human beta-endorphin (beta h-EP) have been synthesized: [Gly31]beta h-EP, [Gly31] beta h-endorphinamide, and [Gly31]beta h-endorphinylglycine. All are more active than beta h-EP in both the guinea pig ileum bioassay and the opiate receptor binding assay. The last two analogs are about twice as active as beta h-EP in an assay for analgesia. Modification at position 31 and extension at the COOH terminus may afford a route toward analogs with even greater biological activity.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.76.7.3276
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1979
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 9
    Online Resource
    Online Resource
    beta-Lipotropin: localization of cells and axons in rat brain by immunocytochemistry.
    Proceedings of the National Academy of Sciences ; 1977
    In:  Proceedings of the National Academy of Sciences Vol. 74, No. 11 ( 1977-11), p. 5155-5158
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 74, No. 11 ( 1977-11), p. 5155-5158
    Abstract: Using specific antisera to human beta-lipotropin, we have visualized cells and axons with beta-lipotropin-like immunoreactivity in rat brain and pituitary. The beta-lipotropin so localized is well delineated and contained in the cytoplasm of cells and in beaded axons. Areas of greatest beta-lipotropin content are hypothalamus (with cell bodies in the medial basal hypothalamus and arcuate regions), periventricular nucleus of the thalamus, ansa lenticularis, zona compacta of the substantia nigra, medial amygdaloid nucleus, zona incerta, periaqueductal central gray area, locus ceruleus, and a few fibers in the reticular formation. The question of the exact relationship of beta-lipotropin and methionine-enkephalin remains open, because some brain areas contain both substances and some areas contain only one or the other.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.74.11.5155
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1977
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 10
    Online Resource
    Online Resource
    Isolation, characterization, and synthesis of a corticotropin-inhibiting peptide from human pituitary glands.
    Proceedings of the National Academy of Sciences ; 1978
    In:  Proceedings of the National Academy of Sciences Vol. 75, No. 9 ( 1978-09), p. 4306-4309
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 75, No. 9 ( 1978-09), p. 4306-4309
    Abstract: A corticotropin-inhibiting peptide (CIP) has been isolated from human pituitary extracts. It consists of 32 amino acids with a proposed sequence identical to residues 7--38 of corticotropin (ACTH). The peptide has been synthesized by the solid-phase method. The melanotropic activity of the peptide is estimated to be 30% of the potency of ACTH. It is devoid of corticosteroidogenic activity but is able to inhibit ACTH-stimulated corticosterone production in isolated rat adrenal cells.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.75.9.4306
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1978
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
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