相关实验视频

Updated: Jan 11, 2026

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

蛋白质酸化与蛋白质降解,氧化和内源性酶活性在死后 Esox lucius 肌肉中的相关性

Ling Hu¹, Yongdong Lei², Xin Guo¹

¹School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832000, China; Key Laboratory of Characteristics Agricultural Product Processing and Quality Control (Co-construction by Ministry and Province)，Ministry of Agriculture and Rural Affairs, School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832000, China; Key Laboratory for Food Nutrition and Safety Control of Xinjiang Production and Construction Corps, School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832000, China.

|November 11, 2025

概括

蛋白质酸化影响 walleye 死亡后的肌肉质量. 肌纤维蛋白 (MP) 和体蛋白 (SP) 酸化的变化与冷藏期间的质地,降解,氧化和酶活性相关.

科学领域:

食品科学食品科学食品科学
生物化学生物化学
死亡后的肌肉生物学

背景情况:

死后肌肉质量恶化会影响鱼的纹理和安全性.
蛋白质酸化是细胞过程中的关键调节机制.
了解鱼类肌肉的死后变化对海鲜行业至关重要.

研究的目的:

为了研究蛋白质酸化与 walleye (Esox lucius) 肌肉质量的死后变化之间的关系.
评估冷藏期间肌纤维蛋白 (MP) 和肉质蛋白 (SP) 的酸化如何发生变化.
为了将这些酸化变化与肌肉质量的关键指标相关联.

主要方法:

鱼在4°C的死后温度下存储.
测量了肌肉质量参数,包括pH值,纹理 (剪切力),蛋白质降解 (MFI),氧化 (碳基,硫基) 和酶活性.
量化了MP和SP的酸化水平.
在酸化和质量参数之间进行了相关性分析.

主要成果:

储存期间肌肉质量下降,由pH值波动,MFI增加,剪切力降低,蛋白质氧化率升高和硫含量降低所证明.
内源蛋白酶仍然活跃,导致肌纤维蛋白质降解.
MP的酸化降低,而SP的酸化随着储存时间的增加而增加.
在MP/SP酸化和肌肉质地,降解,氧化和蛋白酶活性之间发现了显著的相关性.

结论:

蛋白质酸化在调节鱼肌肉质量的死后变化方面发挥着重要作用.
酸化MP和SP的变化与质地,蛋白质完整性和酶活性的变化有关.
这项研究提供了关于在冷藏储存期间控制鱼类肌肉质量的生化机制的见解.

关键词:

内源性酶活性是内源性的.这就是Esox lucius.在死后进行尸检.蛋白质降解蛋白质降解蛋白质的酸化是蛋白质的酸化.质地软化质地软化

更多相关视频

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

Published on: December 14, 2017

相关概念视频

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

Phosphorylation

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

Regulated Protein Degradation

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...