Identification of the modifying sites of mono-PEGylated salmon calcitonins by capillary electrophoresis and MALDI-TOF mass spectrometry

Dong Hee Na; Myung Ok Park; So Yoen Choi; Yong Suk Kim; Seung Seok Lee; Sun Dong Yoo; Hye Suk Lee; Kang Choon Lee

doi:10.1016/S0378-4347(00)00599-5

Identification of the modifying sites of mono-PEGylated salmon calcitonins by capillary electrophoresis and MALDI-TOF mass spectrometry

Dong Hee Na
, Myung Ok Park
, So Yoen Choi
, Yong Suk Kim
, Seung Seok Lee
, Sun Dong Yoo
, Hye Suk Lee
, Kang Choon Lee

Sungkyunkwan University

Research output: Contribution to journal › Article › peer-review

41 Scopus citations

Abstract

A capillary electrophoretic method (CE) was developed for the determination of the PEG-modification sites of three positional isomers of mono-PEG modified salmon calcitonins (mono-PEG-sCTs). Resistance to proteolytic degradation on the PEG modification sites resulted in different patterns of CE electropherograms for the tryptic digested mono-PEG-sCTs isomers, and the PEG modification sites were assigned accordingly. The PEG-modification sites were also confirmed directly by determining the molecular masses of the tryptic digested PEG-modified fragments of respective mono-PEG-sCT by the matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry.

Original language	English
Pages (from-to)	259-263
Number of pages	5
Journal	Journal of Chromatography B: Biomedical Sciences and Applications
Volume	754
Issue number	1
DOIs	https://doi.org/10.1016/S0378-4347(00)00599-5
State	Published - 15 Apr 2001

Bibliographical note

Funding Information:
This work was supported by grant No. 2000-2-21700-001-3 from the Basic Research Program of the Korea Science & Engineering Foundation, and partially by the Brain Korea 21 Program.

Keywords

Calcitonins

Access to Document

10.1016/S0378-4347(00)00599-5

Cite this

Na, D. H., Park, M. O., Choi, S. Y., Kim, Y. S., Lee, S. S., Yoo, S. D., Lee, H. S., & Lee, K. C. (2001). Identification of the modifying sites of mono-PEGylated salmon calcitonins by capillary electrophoresis and MALDI-TOF mass spectrometry. Journal of Chromatography B: Biomedical Sciences and Applications, 754(1), 259-263. https://doi.org/10.1016/S0378-4347(00)00599-5

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title = "Identification of the modifying sites of mono-PEGylated salmon calcitonins by capillary electrophoresis and MALDI-TOF mass spectrometry",

abstract = "A capillary electrophoretic method (CE) was developed for the determination of the PEG-modification sites of three positional isomers of mono-PEG modified salmon calcitonins (mono-PEG-sCTs). Resistance to proteolytic degradation on the PEG modification sites resulted in different patterns of CE electropherograms for the tryptic digested mono-PEG-sCTs isomers, and the PEG modification sites were assigned accordingly. The PEG-modification sites were also confirmed directly by determining the molecular masses of the tryptic digested PEG-modified fragments of respective mono-PEG-sCT by the matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry.",

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note = "Funding Information: This work was supported by grant No. 2000-2-21700-001-3 from the Basic Research Program of the Korea Science \& Engineering Foundation, and partially by the Brain Korea 21 Program.",

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doi = "10.1016/S0378-4347(00)00599-5",

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AU - Na, Dong Hee

AU - Park, Myung Ok

AU - Choi, So Yoen

AU - Kim, Yong Suk

AU - Lee, Seung Seok

AU - Yoo, Sun Dong

AU - Lee, Hye Suk

AU - Lee, Kang Choon

N1 - Funding Information: This work was supported by grant No. 2000-2-21700-001-3 from the Basic Research Program of the Korea Science & Engineering Foundation, and partially by the Brain Korea 21 Program.

PY - 2001/4/15

Y1 - 2001/4/15

N2 - A capillary electrophoretic method (CE) was developed for the determination of the PEG-modification sites of three positional isomers of mono-PEG modified salmon calcitonins (mono-PEG-sCTs). Resistance to proteolytic degradation on the PEG modification sites resulted in different patterns of CE electropherograms for the tryptic digested mono-PEG-sCTs isomers, and the PEG modification sites were assigned accordingly. The PEG-modification sites were also confirmed directly by determining the molecular masses of the tryptic digested PEG-modified fragments of respective mono-PEG-sCT by the matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry.

AB - A capillary electrophoretic method (CE) was developed for the determination of the PEG-modification sites of three positional isomers of mono-PEG modified salmon calcitonins (mono-PEG-sCTs). Resistance to proteolytic degradation on the PEG modification sites resulted in different patterns of CE electropherograms for the tryptic digested mono-PEG-sCTs isomers, and the PEG modification sites were assigned accordingly. The PEG-modification sites were also confirmed directly by determining the molecular masses of the tryptic digested PEG-modified fragments of respective mono-PEG-sCT by the matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry.

KW - Calcitonins

UR - https://www.scopus.com/pages/publications/0035871896

U2 - 10.1016/S0378-4347(00)00599-5

DO - 10.1016/S0378-4347(00)00599-5

M3 - Article

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AN - SCOPUS:0035871896

SN - 1387-2273

VL - 754

SP - 259

EP - 263

JO - Journal of Chromatography B: Biomedical Sciences and Applications

JF - Journal of Chromatography B: Biomedical Sciences and Applications

IS - 1

ER -

Identification of the modifying sites of mono-PEGylated salmon calcitonins by capillary electrophoresis and MALDI-TOF mass spectrometry

Abstract

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Keywords

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