Výsledky vyhledávání - "Dorit Vashdi"

Lactogenic hormones rapidly activate p21 ras /mitogen-activated protein kinase in Nb2-11C rat lymphoma cells

Autor: Dorit Vashdi-Elberg, Micha J. Rapoport, Arieh Gertler, Yoram Shechter, Gerard Elberg

Publikováno v: Endocrine. 4:65-71

Lactogenic hormone-dependent Nb2-11C cells proliferate in response to prolactin (PRL) or human growth hormone (hGH). We have investigated the activation of p21 ras and mitogen-activated protein kinase (MAP-kinase) by hGH in lactogen-dependent Nb2-11C

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cee509f6dbf67d314ad1555e9cef9f94
https://doi.org/10.1007/bf02738876

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Preparation and comparison of biological properties of recombinant carp (Cyprinus carpio) growth hormone and its Cys-123 to Ala mutant

Autor: Nava Chapnik-Cohen, Orli Lipshitz, Avigdor Levanon, Mira Fine, Edna Sakal, Violet Daniel, Arieh Gertler, Dorit Vashdi

Publikováno v: Fish Physiology and Biochemistry. 11:353-361

Carp growth hormone (cGH) cDNA, in which Cys-123 was mutated to Ala, was prepared, transferred to the expression vector, expressed in Escherichia coli and the mutant was purified to homogeneity. The mutation only slightly improved yield of the monome

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f34f9bc5405b00e1f2354035faf78068
https://doi.org/10.1007/bf00004585

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Recombinant Carp (Cyprinus carpio) Growth Hormone: Expression, Purification, and Determination of Biological Activity in Vitro and in Vivo

Autor: Edna Sakal, Avigdor Levanon, Violet Daniel, Orli Lipshitz, Arieh Gertler, Dorit Vashdi, Mira Fine

Publikováno v: General and Comparative Endocrinology. 89:51-61

Carp growth hormone (cGH) cDNA (Koren et al., 1989) was cloned under the control of lambda-phage PLOL promoter and lambda cll ribosomal binding site into pBR322 plasmid to enable its expression in Escherichia coli A1645 that produces constitutively t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::088427423a0d6b988430f9d10f13737a
https://doi.org/10.1006/gcen.1993.1008

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Preparation, purification, and determination of the biological activities of 12 N terminus-truncated recombinant analogues of bovine placental lactogen

Autor: Arieh Gertler, S D Hauser, J J Freeman, Dorit Vashdi, Edna Sakal, G G Krivi, N Staten

Publikováno v: Journal of Biological Chemistry. 267:12655-12659

Removal of 13 to 15 amino acids from the N terminus of bovine placental lactogen (bPL), which according to the three-dimensional structure of pGH corresponds to a nonhelical part of bPL, did not effect its secondary structure or change the monomer co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9c2dd799908c1f223ac4d3a18108e3ba
https://doi.org/10.1016/s0021-9258(18)42327-7

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Selective modification of recombinant bovine placental lactogen by site-directed mutagenesis at its C terminus

Autor: Gwen G. Krivi, Edna Sakal, N.R. Staten, Arieh Gertler, Jean Djiane, Russell E. McKinnie, Dorit Vashdi-Elberg

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1996, 271 (10), pp.5558-5564. ⟨10.1074/jbc.271.10.5558⟩
Journal of Biological Chemistry 10 (271), 5558-5564. (1996)

Five recombinant analogues of bovine placental lactogen (bPL) ((bPL(S184H), bPL(S187A), bPL(S187F), bPL(T188F), bPL(T188F,I190F)) were prepared, expressed in Escherichia coli, and purified to homogeneity. Circular dichroism analysis revealed no or mi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be53e930dae3b51d98a9411dd5133b78
https://hal.inrae.fr/hal-02687643

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N-terminal-truncated recombinant analogs of bovine placental lactogen: interaction with human and rat growth hormone receptors and insulin-like growth factor-I secretion mediated by somatogenic receptors in rat hepatocytes

Autor: Edna Sakal, Gwen G. Krivi, Dorit Vashdi-Elberg, Nicholas R. Staten, Arieh Gertler

Publikováno v: Endocrinology. 136(3)

Bovine placental lactogen (bPL) was found to be as potent as human GH (hGH) in its ability to bind to soluble full-size recombinant hGH-binding protein (hGHBP) and to membrane-embedded hGH receptor in intact IM-9 human lymphocytes. bPL was also capab

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eb1217f2b09494947912e2f65c2237a
https://pubmed.ncbi.nlm.nih.gov/7867580

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Biological activity of bovine placental lactogen in 3T3-F442A preadipocytes is mediated through a somatogenic receptor

Autor: Dorit Vashdi, Edna Sakal, Gerard Elberg, Arieh Gertler

Publikováno v: FEBS Letters. (2):101-104

Bovine placental lactogen (bPL) exhibited antimitogenic differentiation-promoting, biological activity in 3T3-F442A preadipocytes, Competitive binding studies and affinity labelling revealed bPL activity to be mediated through a somatogenic type of r

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