Characterization of disulfide bridges pattern of recombinant human interleukin 12 fusion protein p40 subunit and identification and quantification of cysteinylated free cysteine 252,Rapid Communications in Mass Spectrometry

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Characterization of disulfide bridges pattern of recombinant human interleukin 12 fusion protein p40 subunit and identification and quantification of cysteinylated free cysteine 252
Rapid Communications in Mass Spectrometry ( IF 2 ) Pub Date : 2022-04-12 , DOI: 10.1002/rcm.9313
Antonio Datola _{1,

2} , Maura Melchiorre _{1,

2} , Fabio Baroni _{1,

2} , Luisa Iozzino _{1,

2} , Angelo Palmese _{1,

2}

Affiliation

We show evidence of cysteinylation on Cys252 of recombinant human p40 subunit of interleukin 12 (IL-12). This was reported in 1996. However, no paper detailing this concept has been published yet. Our paper reports the quantification of Cys252 cysteinylation as well as the full disulfide bridges assignment by nonreducing peptide mapping using mass spectrometry (MS) detection.

中文翻译：

重组人白细胞介素 12 融合蛋白 p40 亚基二硫键模式的表征以及半胱氨酸化游离半胱氨酸 252 的鉴定和定量

我们展示了重组人白细胞介素 12 (IL-12) p40 亚基的 Cys252 上半胱氨酸化的证据。这是 1996 年报道的。然而，尚未发表详细介绍这一概念的论文。我们的论文报告了使用质谱 (MS) 检测的非还原肽图对 Cys252 半胱氨酸化的定量以及完整的二硫键分配。

更新日期：2022-04-12

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