甲氨酸在氧化修饰纤维素原蛋白的功能中的作用
L V Yurina1, A D Vasilyeva1, E S Gavrilina1
1N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Russia.
Biochimica et biophysica acta. Proteins and proteomics
|April 6, 2024
概括
纤维素素具有抗氧化应激的保护机制. 氨酸残留物作为抗氧化剂,在轻度至中度氧化条件下保持纤维素原功能.
科学领域:
- 生物化学 生物化学
- 氧化压力研究研究 氧化压力研究
- 蛋白质组学是指蛋白质组学.
背景情况:
- 氧化应激会损害纤维素原的功能,影响血液凝块的形成.
- 纤维素原的抗氧化机制尚未得到充分理解.
- 反应性氧物种 (ROS) 可以导致纤维素原体的有害的翻译后修饰.
研究的目的:
- 为了研究低酸 (HOCl) 度对纤维原体的影响.
- 探索纤维素素对ROS的保护机制.
- 分析纤维素素的氧化变化及其对纤维素网络结构和凝块溶解的影响.
主要方法:
- 纤维素原暴露于不同度的HOCl (10微米和25微米).
- 使用高性能液体染色学-并联质谱法 (HPLC-MS/MS) 分析纤维素原氧化变化.
- 评估纤维素到纤维素的转化和纤维素水解动力学.
主要成果:
- 10微米的HOCl没有影响纤维素原的功能活性,与25微米的HOCl不同.
- 特定的氨酸残留物 (AαMet476, AαMet517, AαMet584, BβMet367, γMet264, γMet94) 被确定为ROS清理剂.
- 这些氨酸残留物起到关键的抗氧化功能,保护纤维素原.
结论:
- 纤维素素具有针对ROS的固有保护机制.
- 氨酸残留物作为ROS清理剂,保持纤维素原的完整性和在氧化应激下的功能.
- 该研究揭示了纤维素原对有害ROS作用的适应性,这对于氧化环境中的血液功能至关重要.
关键词:
抗氧化剂是甲氨酸.与焦点相对应的激光扫描显微镜.纤维素纤维素是一种纤维素.纤维素原蛋白是一种纤维素.纤维化解是一种纤维化解.在HPLC-MS/MS中使用.过酸盐诱导的氧化过程氧化性修饰是指氧化性修饰.更多相关视频
07:16Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
1.7K
05:57Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
Published on: April 26, 2024
377
相关概念视频
Protein Modifications in the RER
5.1K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.1K
Amyloid Fibrils
9.5K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.5K
Covalently Linked Protein Regulators
6.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.8K
Transfer RNA Synthesis
11.9K
One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
11.9K
Globular and Fibrous Proteins
43.7K
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
43.7K
Protein and Protein Structure
79.5K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
79.5K
