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MALDI-TOF-MS Characterization of N-linked Glycoprotein Derived From Ginger With ACE Inhibitory Activity

MALDI-TOF-MS Characterization of N-linked Glycoprotein Derived From Ginger With ACE Inhibitory Activity

Wenzhu Zhao, Yuejiao Chen, Siyu Xue, Zhipeng Yu, Hanjie Yu, Jingbo Liu, Jianrong Li, Feng Chen

Food Funct. 2018 May 23;9(5):2755-2761.

PMID: 29671439

Abstract:

Herein, the ability of ginger glycoproteins to inhibit the angiotensin-converting enzyme (ACE) is characterized. The activity is monitored via HPLC, and then the crude glycoproteins are enriched with lectin microarrays and magnetic microspheres. The N-linked glycans released from the enriched glycoproteins by PNGase F are identified by MALDI-TOF-MS. The results suggest that the crude ginger glycoproteins are active against ACE with an IC50 value of 0.83 ± 0.09 mg mL-1. The ginger glycoproteins are enriched by concanavalin A (Con A) and solanum tuberosum (Potato) lectin (STL), and the structures of the N-glycans released from the ginger glycoproteins include high-mannose type glycans, fucosylated-type glycans, and hybrid-type glycans, as analyzed by MALDI-TOF-MS. The results of this study are expected to provide a reference for the glycan structure of ginger glycoproteins with ACE-inhibitory activity.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42417983	Lectin from Solanum tuberosum (potato)			Price

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