相关实验视频

Updated: May 23, 2025

Measurement of Calcium Fluctuations Within the Sarcoplasmic Reticulum of Cultured Smooth Muscle Cells Using FRET-based Confocal Imaging

Measurement of Calcium Fluctuations Within the Sarcoplasmic Reticulum of Cultured Smooth Muscle Cells Using FRET-based Confocal Imaging

Published on: June 20, 2016

对加工和食品矩阵对结构的影响的洞察力,以及对肉质结合蛋白的ELISA检测

Wenye Zhu¹, Qingwen Liu¹, Yuhao Huang¹

¹State Key Laboratory of Marine Food Processing & Safety Control, College of Food Science and Engineering, Ocean University of China, Huangdao Campus, No.1299, Sansha Road, Qingdao, Shandong Province, 266000, PR China.

|March 8, 2025

概括

研究了食物矩阵对肉质结合蛋白 (SCP) 检测的影响. 间接竞争型ELISA (icELISA) 比三明治ELISA (sELISA) 对食物矩阵干扰的抵抗力更强.

科学领域:

食品分析和免疫测试的发展.
复杂矩阵中的蛋白质结构-功能关系.

背景情况:

针对肉质结合蛋白 (SCP) 的三明治ELISA (sELISA) 对食物矩阵敏感,但基本机制尚不清楚.
准确量化SCP对于食品质量和安全评估至关重要.

研究的目的:

阐明环境因素,食品矩阵和加工对SCP结构和ELISA检测能力的综合影响.
为了比较sELISA和间接竞争ELISA (icELISA) 的干扰阻力,用于SCP检测.

主要方法:

对SCP进行了不同温度,pH值和不同食物矩阵 (无机盐,碳水化合物,花生油) 的测试.
测试包括sELISA,icELISA,电泳,多光谱技术和分子模拟.
分析了SCP的结构变化及其对免疫试验性能的影响.

主要成果:

高温 (>80°C对于sELISA,>100°C对于icELISA) 导致SCP展开,抑制了检测回收.
酸性条件导致SCP紧缩,增强了icELISA,但降低了sELISA的性能.
无机盐,碳水化合物和花生油通过非共价相互作用显著改变了SCP的三级结构和聚合,影响了ELISA结果.
与sELISA相比,icELISA对矩阵干扰具有更强的抗性,这可能是由于表位组的保存.

结论:

环境因素和食物矩阵显著影响SCP结构和ELISA的检测.
非共价相互作用在SCP的矩阵诱导的结构变化中起着关键作用.
与sELISA相比,icELISA在SCP量化中提供了对食物矩阵干扰的优越稳定性.

关键词:

甲类过敏原检测检测器艾丽莎·伊丽莎·伊丽莎矩阵干扰是对矩阵的干扰.处理处理处理蛋白质结构蛋白质结构石灰结合蛋白质的萨科普拉斯米细胞.

更多相关视频

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+

Published on: May 19, 2017

Monitoring Endoplasmic Reticulum Calcium Homeostasis Using a Gaussia Luciferase SERCaMP

Monitoring Endoplasmic Reticulum Calcium Homeostasis Using a Gaussia Luciferase SERCaMP

Published on: September 6, 2015

相关概念视频

Calmodulin-dependent Signaling

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

Feedback Regulation of Calcium Concentration

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...