Výsledky vyhledávání - "John L. Morell"

Solid phase synthesis of ovine corticotropin releasing factor

Publikováno v: International Journal of Peptide and Protein Research. 26:49-54

Ovine corticotropin releasing factor was synthesized by the stepwise solid phase method under conditions anticipated to maximize yield. Final yields of fully active hormone were 34% based on peptide which could be removed from the resin and 24% on in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::881aed4117478fce280c17eae002896b
https://doi.org/10.1111/j.1399-3011.1985.tb03176.x

Zobrazit plný text záznamu

Formation of aminosuccinyl derivative from β-phenacyl aspartyl peptides catalyzed by sodium thiophenoxide

Autor: Pierrette Gaudreau, John L. Morell, Erhard Gross

Publikováno v: International Journal of Peptide and Protein Research. 19:280-283

In the solid-phase synthesis of cholecystokinin 30-33, Trp-Met-Asp-Phe- amide, the beta-phenacyl ester was used to protect the beta-carboxyl of aspartyl residue. The ester was cleaved, on the solid support, with a 1 M solution of sodium thiophenoxide

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d404236952f90bae84b26de06d7426d
https://doi.org/10.1111/j.1399-3011.1982.tb03039.x

Zobrazit plný text záznamu

Cleavage of aspartyl β-phenacyl esters by selenophenol under neutral conditions

Autor: Erhard Gross, Pierrette Gaudreau, John L. Morell

Publikováno v: International Journal of Peptide and Protein Research. 19:487-489

Neutral selenophenol in DMF accomplished the removal of the beta-phenacyl protecting group of aspartic acid in solution, on the peptide Boc-Asp (beta-OPac)- Phe amide and on the resin peptide Boc-Trp(Nin-For)-Met-Asp (beta-OPac)-P (CCK 30-33) without

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33a4537372429c467fa6f7030b1f0e98
https://doi.org/10.1111/j.1399-3011.1982.tb02633.x

Zobrazit plný text záznamu

The reaction of cyanogen bromide with S-methylcysteine: Fragmentation of the peptide 14–29 of bovine pancreatic ribonuclease A

Autor: John L. Morell, Erhard Gross

Publikováno v: Biochemical and Biophysical Research Communications. 59:1145-1150

Summary The S-methylated peptide 14–29 of bovine pancreatic ribonuclease A is cleaved by cyanogen bromide with the formation of the expected fragments in 88% yield based on the conversion of S-methylcysteine.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::081fe98738f134463f3c7fc9c86454ae
https://doi.org/10.1016/s0006-291x(74)80098-7

Zobrazit plný text záznamu

Properties and regulation of high-affinity pituitary receptors for corticotropin-releasing factor

Autor: Peter C. Wynn, Greti Aguilera, John L. Morell, Kevin J. Catt

Publikováno v: Biochemical and Biophysical Research Communications. 110:602-608

Specific receptors for corticotropin-releasing factor (CRF) were identified in the rat anterior pituitary gland by binding studies with 125I-Tyr-CRF. Binding of the labeled CRF analog to pituitary particles was rapid and temperature-dependent, and re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a527d62bc20f27701eb1b71eae1fb41
https://doi.org/10.1016/0006-291x(83)91192-0

Zobrazit plný text záznamu

Mechanisms of action of corticotropin-releasing factor and other regulators of corticotropin release in rat pituitary cells

Autor: John L. Morell, J X Wilson, Kevin J. Catt, Greti Aguilera, J H Brown, James P. Harwood

Publikováno v: Journal of Biological Chemistry. 258:8039-8045

The role of cyclic AMP in the stimulation of corticotropin (ACTH) release by corticotropin-releasing factor (CRF), angiotensin II (AII), vasopressin (VP), and norepinephrine (NE) was examined in cultured rat anterior pituitary cells. Synthetic CRF ra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::778f52a370b7cc239918a41da75fad3b
https://doi.org/10.1016/s0021-9258(20)82024-9

Zobrazit plný text záznamu

The number and nature of α,β-unsaturated amino acids in nisin

Autor: Erhard Gross, John L. Morell

Publikováno v: FEBS Letters. 2:61-64

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4526cd7cc7e96a81aacc6df73241d00d
https://doi.org/10.1016/0014-5793(68)80101-2

Zobrazit plný text záznamu

DEHYDROALANYLLYSINE: IDENTICAL COOH-TERMINAL STRUCTURES IN THE PEPTIDE ANTIBIOTICS NISIN AND SUBTILIN

Autor: John L. Morell, Erhard Gross, Lyman C. Craig

Publikováno v: Proceedings of the National Academy of Sciences. 62:952-956

The recent finding of alpha,beta-unsaturated amino acid residues by Gross and Morrel in the polypeptide antibiotic nisin has stimulated a wider investigation of other antibiotic peptides, particularly those known to contain lanthionine. Subtilin is s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c1286de16244a3b227c584577174415
https://doi.org/10.1073/pnas.62.3.952

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání