Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Edna Sakal"'
Publikováno v:
Preparative Biochemistry and Biotechnology. 30:107-123
The cDNA of the extracellular domain of rabbit growth hormone receptor (rbGHR-ECD) was cloned in the prokaryotic expression vector pMON, to enable its expression in Escherichia coli after induction with nalidixic acid. The bacterially expressed rbPRL
Autor:
C Bignon, Edna Sakal, Arieh Gertler, Jean Djiane, N Daniel, J Paly, N Chapnik-Cohen, L Belair
Publikováno v:
Journal of Endocrinology
Journal of Endocrinology, BioScientifica, 1998, 159 (3), pp.509-518. ⟨10.1677/joe.0.1590509⟩
Journal of Endocrinology 3 (159), 509-518. (1998)
Journal of Endocrinology, BioScientifica, 1998, 159 (3), pp.509-518. ⟨10.1677/joe.0.1590509⟩
Journal of Endocrinology 3 (159), 509-518. (1998)
International audience; Caprine placental lactogen (cPL) cDNA was cloned by reverse transcription (RT)-PCR from total RNA of goat placenta. The PCR product encoding for the mature protein was gel purified, ligated to pGEM-T and finally subcloned into
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
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
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
Publikováno v:
Archives of Insect Biochemistry and Physiology. 20:157-164
Polyclonal antibodies were produced against trypsin-like enzyme TLE-2, one of two trypsins isolated from the midgut cecae of the locust Locusta migratoria. Using those antibodies a heterologous RIA was developed. The specificity of the antibodies was
Publikováno v:
Biochemistry. 30:8899-8904
Modification of human growth hormone (hGH) with a low equimolar concentration of fluorescein isothiocyanate (FITC) yielded a derivative containing 1 mol of fluorescein/mol of protein. The site of modification was identified as lysine-70. Lysine-70 of
Publikováno v:
Molecular and Cellular Endocrinology. 80:183-192
The ortho, meta, and para forms of hydroxyphenyl acetate were found to be inhibitory in the order of ortho > para > meta in three distinct biological assays: (a) insulin-dependent assimilation of glucose into lipids in intact adipocytes, (b) growth a
Autor:
Edna Sakal, Arieh Gertler, A Kantor, C Bignon, S. W. Rowlinson, Daniel Helman, Jean Djiane, J Grosclaude, R Shapira, C Nespoulous, H Leibovitch, A Shamay
Publikováno v:
Journal of Endocrinology
Journal of Endocrinology, BioScientifica, 1997, 152, pp.317-327
Journal of Endocrinology, BioScientifica, 1997, 152, pp.317-327
To clone ovine placental lactogen (oPL) cDNA, total RNA from sheep placental cotyledon was reverse transcribed and the single-stranded cDNA was PCR-amplified with 5′ and 3′ primers containing, respectively, Ncol and PstI sites. The oPL cDNA fragm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c4e5ce0cb02681849ca092b00b69e46
https://hal.inrae.fr/hal-02695619
https://hal.inrae.fr/hal-02695619
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)
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
https://hal.inrae.fr/hal-02687643