Journal
BIOTECHNOLOGY & BIOTECHNOLOGICAL EQUIPMENT
Volume 23, Issue -, Pages 718-721Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/13102818.2009.10818525
Keywords
glycoprotein; Cu/Zn superoxide dismutase; MALDI-TOF-TOF; Q-Trap; yeast Kluyveromyces marxianus
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Funding
- National Science Fund, Bulgarian Ministry of Education and Science [(sic)-BY201/06-2492]
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The primary structure of Cu/Zn SOD from Kluyveromyces marxianus NBIMCC 1984 (Cu/Zn-KmSOD) was elucidated by N-terminal sequencing of the intact protein and by determination of the amino acid sequences of the tryptic peptides through MALDI-TOF-TOF. The molecular mass of the SOD homodimer subunit, containing 152 amino acid residues, was calculated to be 15858,3 Da while by MALDI-TOF 17096,63 Da were determined. Only one typtophan residue at position 33 and one linkage site -Asn-Ile/Leu-Thr-were identified in the polypeptide chain of Cu/Zn-KmSOD. The full oligosaccharide structure of the naturally glycosylated superoxide dismutase was determined by mass spectrometry. Enzymatialyc liberated N-glycan from the enzyme was analysed using MALDI-TOF and tandem mass spectrometry on a Q-Trap mass spectrometer. One methylated hexose and an external fucose, linked to the hexoses were identified in the glycan.
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