Isolation, characterization, and stability of positional isomers of mono-PEGylated salmon calcitonins

Pharmaceutical Research

Volumn 16, Issue 6, 1999, Pages 813-818

  Lee, Kang Choon ^a   Moon, Seung Cheol ^a   Park, Myung Ok ^a   Lee, Jung Tae ^a   Na, Dong Hee ^a   Yoo, Sun Dong ^a   Lee, Hye Suk ^b   DeLuca, Patrick P ^c  

^a Sungkyunkwan University   (South Korea)

^b Wonkwang University   (South Korea)

^c University of Kentucky   (United States)

Author keywords

Calcitonin; HPLC; PEGylation; Peptide; Polyethylene glycol; Stability; Tryptic digestion

Indexed keywords

MACROGOL; SALCATONIN;

ANIMAL TISSUE; ARTICLE; DRUG DEGRADATION; DRUG HALF LIFE; DRUG ISOLATION; DRUG STABILITY; DRUG STRUCTURE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ISOMER; KIDNEY HOMOGENATE; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; RAT;

AMINO ACID SEQUENCE; ANIMALS; CALCITONIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; PROTEIN ISOFORMS; RATS; SALMON;

EID: 0033055121     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1018861616465     Document Type: Article

References (30)

1. 1. M. Azria. The Calcitonins. Physiology and Pharmacology, Karger, Basel, 1989.
2. 2. K. C. Lee, E. E. Soltis, P. S. Newman, K. W. Burton, R. C. Mehta, and P. P. DeLuca. In vivo assessment of salmon calcitonin sustained release from biodegradable micropsheres. J. Contr. Rel. 17:199-206 (1991).
3. 3. E. Compston. Prevention and management of osteoporosis. Current trends and future prospects. Drugs 53:727-35 (1997).
4. 4. G. Segra and P. Dal Pra. Calcitonin pharmacokinetics. In A. Pecile (ed.), Calcitonin, Excerpta Medica, Amsterdam, 1985, pp. 99-107.
5. 5. K. C. Lee, Y. J. Lee, H. M. Song, C. J. Chun, and P. P. DeLuca. Degradation of synthetic salmon calcitonin in aqueous solution. Pharm. Res 9:1521-1523 (1992).
6. 6. H. S. Lee, J. S. Lee, H. Lee, Y. S. Jung, P. P. DeLuca, and K. C. Lee. Reversed-phase high-performance liquid chromatography of salmon calcitonin and its degradation products in biological sample using column switching and flow-through radioisotope detection. J. Chromatogr. B. 673:136-141 (1995).
7. 7. J. Hysing, J. O. Gordeladze, G. Christensen, and H. Tolleshaug. Renal uptake and degradation of trapped-label calcitonin. Biochem. Pharmacol. 41:1119-1126 (1991).
8. 8. R. E. Simmons, J. T. Hjelle, C. A. Mahoney, L. J. Deftos, W. Lisker, P. Kato, and R. Rabkin. Renal metabolism of calcitonin. Am. J. Physiol. 254:F593-F600 (1988).
9. 9. S. R. Lang, W. Staudenmann, P. James, H. Manz, R. Kessler, B. Galli, H. Moser, A. Rummelt, and H. P. Merkle. Proteolysis of human calcitonin in excised bovine nasal mucosa: Elucidation of the metabolic pathway by liquid secondary ionization mass spectrometry (LSIMS) and matrix assisted laser desorption ionization mass spectrometry (MALDI). Pharm. Res. 13:1679-1685 (1996).
10. 10. V. Windisch, F. DeLuccia, L. Duhau, F. Herman, J. J. Mencel, S. Tang, and M. Vuilhorgne. Degradation pathways of salmon calcitonin in aqueous solution. J. Pharm. Sci. 86:359-364 (1997).
11. 11. G. E. Francis, C. Delgado, and D. Fisher. PEG-modified proteins. In T. J. Ahern and M. C. Manning (eds.), Stability of Protein Pharmaceuticals, Part B: In vivo pathways of degradation and strategies for protein stabilization. Plenum Press, New York, 1992, pp. 235-263.
12. 12. N. V. Katre. The conjugation of proteins with polyethylene glycol and other polymers (Altering properties of proteins to enhance their therapeutic potential). Adv. Drug Del. Rev. 10:91-114 (1993).
13. 13. Y. Inada, A. Matsushima, M. Hiroto, H. Nishimura, and Y. Kodera. Modification of proteins with polyethylene glycol derivatives. Methods Enzymol. 242:65-90 (1994).
14. 14. S. Zalipsky. Chemistry of polyethylene glycol conjugates with biologically active molecules. Adv. Drug Del. Rev. 16:157-182 (1995).
15. 15. F. M. Veronese, C. Monfardini, P. Caliceti, O. Schiavon, M. D. Scrawen, and D. Beer. Improvement of pharmacokinetic, immunological and stability properties of asparaginase by conjugation to linear and branched monomethoxy poly(ethylene glycol). J. Contr. Rel. 40:199-209 (1996).
16. 16. Y. Tsutsumi, S. Tsunoda, H. Kamada, T. Kihira, S. Nakagawa, Y. Kaneda, T. Kanamori, and T. Mayumi. Molecular design of hybrid tumor necrosis factor-α II: the molecular size of polyethylene glycol-modified tumor necrosis factor-α affects its antitumor potency. Brt. J. Cancer 74:1090-1095 (1996).
17. 17. P. McGoff, A. C. Baziotis, and R. Maskiewicz. Analysis of polyethylene glycol modified superoxide dismutase by chromatographic, electrophoretic, light scattering, chemical and enzymatic methods. Chem. Pharm. Bull 36:3079-3091 (1988).
18. 18. M. Kunitani, G. Dollinger, D. Johnson, and L. Kresin. On-line characterization of polyethylene glycol-modified proteins. J. Chromatogr. 588:125-137 (1991).
19. 19. J. Snider, C. Neville, L. Yuan, and J. Bullock. Characterization of the heterogenicity of polyethylene glycol-modified superoxide dismutase by chromatographic and electrophoretic techniques. J. Chromatogr. 599:141-155 (1992).
20. 20. D. H. Na, B. H. Woo, and K. C. Lee. Quantitative analysis of derivatized proteins prepared with pyridyl disulfide-containing cross-linkers by HPLC. Bioconj. Chem. 10: in press
21. 21. R. J. Goodson and N. V. Katre. Site-directed PEGylation of recombinant interleukin-2 at its glycosylation site. Biotechnology 8:343-346 (1990).
22. 22. H. F. Gaertner and R. E. Offord. Site-specific attachment of functionalized poly(ethylene glycol) to the amino terminus of proteins. Bioconj. Chem. 7:38-44 (1996).
23. 23. O. B. Kinstler, D. N. Brems, S. L. Lauren, A. G. Paige, J. B. Hamburger, and M. J. Treuheit. Characterization and stability of N-terminally PEGylated rhG-CSF. Pharm. Res. 13:996-1002 (1995).
24. 24. A. M. Felix, Y. Lu, and R. M. Campbell. Pegylated peptides IV. Enhanced biological activity of site-directed pegylated GRF analogs. Int. J. Peptide Protein Res. 46:253-264 (1995).
25. 25. S. P. Monkarch, Y. Ma, A. Aglione, P. Bailon, D. Ciolek, B. DeBarbieri, M. C. Graves, K. Hollfelder, H. Michel, A. Palleroni, J. E. Porter, E. Russonman, S. Roy, and Y. E. Pan. Positional isomers of monopegylated interferon α-2a: Isolation, characterization, and biological activity. Anal. Biochem. 247:434-440 (1997).
26. 26. K. C. Lee, K. K. Tak, M. O. Park, J. T. Lee, B. H. Woo, S. D. Yoo, H. S. Lee, and P. P. DeLuca. Preparation and characterization of polyethylene glycol-modified salmon calcitonins. Pharm. Dev. Tech. 4:269-275(1999).
27. 27. K. C. Lee, T. S. Kang, B. H. Woo, J. T. Lee, H. S. Lee, and P. P. DeLuca. Reversed-phase high-performance liquid chromatography of radioiodinated salmon calcitonins. J. Chromatogr. B. 694:31-37 (1997).
28. 28. J. Kajihara, K. Shibata, Y. Nakano, S. Nishimuro, and K. Kato. Physicochemical characterization of PEG-PPG conjugated human urokinase. Biochem. Biophys. Acta 1199:202-208 (1994).
29. 29. R. Clark, K. Olson, G. Fuh, M. Marian, D. Mortensen, G. Teshima, S. Chang, H. Chu, V. Mukku, E. Canova-Davis, T. Somers, M. Cronin, M. Winkler, and J. A. Wells. Long-acting growth hormones produced by conjugation with polyethylene glycol. J. Biol. Chem. 271:21969-21977 (1996).
30. 30. K. C. Lee, J. T. Lee, B. H. Woo, S. C. Moon, and P. P. DeLuca. Analysis of PEGylated salmon calcitonins by radioimmunoassay and HPLC with flow through radioisotope detection. Pharm. Res. 14:S350-351 (1997).