Determination of the structure of ovalbumin glycopeptide AC-B by 1H nuclear magnetic resonance spectroscopy at 500 MHz期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

Determination of the structure of ovalbumin glycopeptide AC-B by 1H nuclear magnetic resonance spectroscopy at 500 MHz

Authors:	Costante Ceccarini Patrizia Lorenzoni Paul H. Atkinson

Affiliation:	Sclavo Research Center, Via Fiorentina 1 53100 Siena, Italy;Albert Einstein College of Medicine Bronx, N.Y., U.S.A.

Abstract:	Three unique, unmodified ovalbumin glycopeptides were separated to homogeneity by high-pressure liquid chromatography. The nuclear magnetic resonance data, at 500 MHz, confirmed the structure of two of the three species and for the first time established the presence of a Man₈GlcNAc₂Asn glycopeptide in ovalbumin. This compound was a single homogeneous isomeric form out of three possible compounds expected as processing intermediates.

Keywords:	Author to whom correspondence should be sent.
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