Matrix-assisted laser desorption mass spectrometric analysis of a pegylated recombinant protein

E. Watson; B. Shah; R. DePrince; R. W. Hendren; R. Nelson

Matrix-assisted laser desorption mass spectrometric analysis of a pegylated recombinant protein

E. Watson, B. Shah, R. DePrince, R. W. Hendren, R. Nelson

Biodesign Institute

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

32 Scopus citations

Abstract

Matrix-assisted laser desorption ionization mass spectrometry (MALDI) has been investigated as a technique for the characterization of recombinant stem cell factor that had been covalently modified with polyethylene glycol (PEG) chains. The attachment of PEG chains produces a heterogeneous mixture of protein species that differ by 6000 Da. These differences in molecular weight could be readily determined by MALDI. The potential of MALDI as a general strategy for characterizing PEG-modified proteins is discussed.

Original language	English (US)
Pages (from-to)	278-281
Number of pages	4
Journal	BioTechniques
Volume	16
Issue number	2
State	Published - Jan 1 1994

ASJC Scopus subject areas

Biotechnology
Biochemistry, Genetics and Molecular Biology(all)

Cite this

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title = "Matrix-assisted laser desorption mass spectrometric analysis of a pegylated recombinant protein",

abstract = "Matrix-assisted laser desorption ionization mass spectrometry (MALDI) has been investigated as a technique for the characterization of recombinant stem cell factor that had been covalently modified with polyethylene glycol (PEG) chains. The attachment of PEG chains produces a heterogeneous mixture of protein species that differ by 6000 Da. These differences in molecular weight could be readily determined by MALDI. The potential of MALDI as a general strategy for characterizing PEG-modified proteins is discussed.",

author = "E. Watson and B. Shah and R. DePrince and Hendren, {R. W.} and R. Nelson",

year = "1994",

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AU - Shah, B.

AU - DePrince, R.

AU - Hendren, R. W.

AU - Nelson, R.

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N2 - Matrix-assisted laser desorption ionization mass spectrometry (MALDI) has been investigated as a technique for the characterization of recombinant stem cell factor that had been covalently modified with polyethylene glycol (PEG) chains. The attachment of PEG chains produces a heterogeneous mixture of protein species that differ by 6000 Da. These differences in molecular weight could be readily determined by MALDI. The potential of MALDI as a general strategy for characterizing PEG-modified proteins is discussed.

AB - Matrix-assisted laser desorption ionization mass spectrometry (MALDI) has been investigated as a technique for the characterization of recombinant stem cell factor that had been covalently modified with polyethylene glycol (PEG) chains. The attachment of PEG chains produces a heterogeneous mixture of protein species that differ by 6000 Da. These differences in molecular weight could be readily determined by MALDI. The potential of MALDI as a general strategy for characterizing PEG-modified proteins is discussed.

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Matrix-assisted laser desorption mass spectrometric analysis of a pegylated recombinant protein

Abstract

ASJC Scopus subject areas

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