Biologically active, derivatizable salmon calcitonin analog: Design, synthesis, and applications

Nicholson, G.C., Moseley, J.M., Evans, T., Martin, T.J. and Kemp, B.E. (1988) Biologically active, derivatizable salmon calcitonin analog: Design, synthesis, and applications. Endocrinology, 123 3: 1483-1488.


Author Nicholson, G.C.
Moseley, J.M.
Evans, T.
Martin, T.J.
Kemp, B.E.
Title Biologically active, derivatizable salmon calcitonin analog: Design, synthesis, and applications
Journal name Endocrinology   Check publisher's open access policy
ISSN 0013-7227
1945-7170
Publication date 1988-09
Sub-type Article (original research)
Volume 123
Issue 3
Start page 1483
End page 1488
Total pages 6
Place of publication Chevy Chase, MD, United States
Publisher The Endocrine Society
Language eng
Formatted abstract
An analog of salmon calcitonin (sCT) has been synthesized, substituting Arg at positions 11 and 18 and Lys at position 14 to provide a free amino group for derivatization. The potency of [Argl1,18Lys14]sCT was equivalent to that of sCT in activating adenylate cyclase in UMR 106-06 cells. The analog was derivatized with biotin, fluorescein, or 4-azidobenzoate without loss of activity. The derivatized analog was not degraded by lysine-specific endoprotease, whereas the underivatized [Argl1,18Lys14]sCT was cleaved at Lys-14. The derivatized analogs were purified by HPLC and subsequently shown to possess full biological activity. The photoactive analog was used to photolabel 88,000 and 71,000 mol wt components of the calcitonin receptor in rat osteoclasts, but only an 88,000 mol wt component was photolabeled in the UMR 106-06 cells.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
 
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