Structure Determination of N-Terminal-blocked Peptide from Hog Kidney Aldose 1-Epimerase by Tandem Mass Spectrometry

The blocked-N-terminal structure of hog kidney aldose 1- epimerase (mutarotase, EC 5.1.3.3) was determined to be Ac-Val-Ser-Val-Thr-Arg-Ser-Val-Phe-Gly-Asp··· by a coupling of conventional methods (enzymatic digestion, amino acid analysis, and Edman sequencing) and tandem mass spectrometry. The side...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1993, Vol.57 (10), p.1772-1774
Hauptverfasser:	Nakamura, Takemichi, Kinoshita, Takeshi, Kitazawa, Satoru, Kimura, Atsuo, Chiba, Seiya
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Arginine - chemistry Biological and medical sciences Biotechnology Carbohydrate Epimerases - chemistry Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Isomerases Kidney - enzymology Mass Spectrometry Molecular Sequence Data Swine
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Zusammenfassung:	The blocked-N-terminal structure of hog kidney aldose 1- epimerase (mutarotase, EC 5.1.3.3) was determined to be Ac-Val-Ser-Val-Thr-Arg-Ser-Val-Phe-Gly-Asp··· by a coupling of conventional methods (enzymatic digestion, amino acid analysis, and Edman sequencing) and tandem mass spectrometry. The side-chain fragmentations observed in the high-energy product ion spectra gave unambiguous sequence information about the arginine-containing N-terminal structure.
ISSN:	0916-8451 1347-6947
DOI:	10.1271/bbb.57.1772