Effect of nitric oxide on conformational changes of ovalbumin accompanying self-assembly into non-disease-associated fibrils

You, Dong-Ju; Lee, Ju Huck; Kim, Jin Young; Jhon, Gil‐Ja; Jung, Hyun Suk

doi:10.1016/j.niox.2015.02.004

Cited by 2 publications

(2 citation statements)

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“…The acidic variant observed for the doubly phosphorylated form with a mass offset of +29 Da, potentially corresponds to S-nitrosylation of a cysteine. Cysteine S-nitrosylation was previously reported on ovalbumin and was related to polymerization of the protein . Sialylated species were detected as highly retained charge variants with intact mass analysis, suggesting the presence of the N -acetylneuraminic acid (NANA) form of sialic acid present on the N -glycans.…”

Section: Resultsmentioning

confidence: 79%

“…Cysteine Snitrosylation was previously reported on ovalbumin and was related to polymerization of the protein. 44 Sialylated species were detected as highly retained charge variants with intact mass analysis, suggesting the presence of the N-acetylneuraminic acid (NANA) form of sialic acid present on the N-glycans. Various NANA-containing forms were found for the doubly phosphorylated ovalbumin as well as for its fragmentation product.…”

Section: Analysis Of Charge Variant Heterogeneitymentioning

confidence: 99%

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Cracking Proteoform Complexity of Ovalbumin with Anion-Exchange Chromatography–High-Resolution Mass Spectrometry under Native Conditions

et al. 2019

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Posttranslational modifications of proteins play fundamental roles in protein function in health and disease. More than 600 different types of posttranslational modifications are known, many of them being of extremely low abundance, causing subtle changes in physicochemical properties and posing an extreme challenge to analytical methods required for their characterization. Here, we report the development of a novel pH gradient-based anion-exchange chromatography method, which can be directly interfaced to Orbitrap-based mass spectrometry for the comprehensive characterization of proteoforms at the intact protein level under native conditions. The analysis of four different proteins demonstrates outstanding chromatographic selectivity, while the mass spectra obtained are of excellent quality enabling the identification of proteoforms, including near isobaric variants, spanning 4 orders of magnitude in abundance. An in-depth analysis of ovalbumin from chicken egg white yields the identification and relative quantification of more than 150 different proteoforms, including fragmented and dimeric forms. More than 20 different ovalbumin charge variants together with their glycoform distributions are identified and quantified, many of which have not been reported previously.

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Section: Resultsmentioning

confidence: 79%

Section: Analysis Of Charge Variant Heterogeneitymentioning

confidence: 99%