AI Article Synopsis
- Nitric oxide (NO) was produced during the oxidation of oxymyoglobin by nitrite, and its levels were continuously measured using a NO-selective electrode system.
- When 500 microM nitrite was introduced to a solution containing oxymyoglobin, the oxidation process was sigmoidal, with a rapid initial release of NO that peaked around 30 microM before declining.
- Increasing the nitrite concentration further accelerated both the production rate of NO and the oxidation of oxymyoglobin, indicating that NO plays a significant role in this oxidation process.
Article Abstract
We found that nitric oxide (NO) was produced during the oxidation of oxymyoglobin by nitrite, by using a NO-selective electrode system, which enabled us to measure NO in phosphate solution, continuously and quantitatively. When 500 microM nitrite was added in the solution of oxymyoglobin (65 microM in heme), oxymyoglobin was oxidized to metmyoglobin in a sigmoidal manner. During the reaction, NO was generated quickly at the initial lag phase, and reached its peak (NO approximated to 30 microM), before the burst oxidation of oxymyoglobin occurred. Then, NO content was gradually decreased. By the addition of the increased concentration of nitrite (1 mM or 2 mM) to oxymyoglobin solution (65 microM in heme), the production rate of NO was much accelerated and the amounts of NO were increased, in good accordance with the accelerated oxidation of oxymyoglobin by nitrite. These results suggest that NO is involved in the oxidation of oxymyoglobin by nitrite.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1620/tjem.182.61 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Understanding metabolic responses to forearm arterial occlusion measured with two-channel broadband near-infrared spectroscopy.
J Biomed Opt
November 2024
University of Texas at Arlington, Department of Bioengineering, Arlington, Texas, United States.
Article Synopsis
- Broadband near-infrared spectroscopy (bbNIRS) is a technique that measures cerebral metabolism but hasn't been widely applied in other biomedical fields.
- The study aimed to track the responses of mitochondrial oxidized cytochrome c oxidase during and after a 5-minute forearm artery blockage, using 14 healthy participants.
- Results showed that while hemodynamic responses changed during occlusion, the levels of cytochrome c oxidase remained steady, suggesting that local oxygen supply supports mitochondrial function even when blood flow is restricted for a short period.
Effects of Oxidized Soybean Meal and Oxidized Soybean Oil on the Muscle Oxidative Stability, Flesh Quality, Amino Acid Profile, and Fatty Acid Profile of .
Antioxidants (Basel)
November 2024
College of Marine and Biology Engineering, Yancheng Institute of Technology, Yancheng 224051, China.
This study aimed to investigate the effects of oxidized soybean meal and oxidized soybean oil on the muscle oxidative stability, flesh quality, amino acid profile, and fatty acid profile of blunt snout bream . Oxidized soybean meal and oxidized soybean oil were obtained from fresh soybean meal (FSM) and fresh soybean oil (FSO) by heating. In the experimental diet, the proportions of oxidized soybean meal (OSM) and oxidized soybean oil (OSO) were 30% and 4.
View Article and Find Full Text PDFL-lysine enhances pork color through antioxidant activity and myoglobin conformational changes.
Food Res Int
December 2024
School of Tourism and Cuisine, Yangzhou University, Yangzhou 225127, China; Key Laboratory of Chinese Cuisine Intangible Cultural Heritage Technology Inheritance, Ministry of Culture and Tourism, Yangzhou, China. Electronic address:
This study aimed to investigate the effect of L-lysine (Lys) on the color of pork and reveal the possible mechanism. The results showed that the L* and a* values increased from 53.69 to 56.
View Article and Find Full Text PDFEffects of polyphenols in combination with L-cysteine/L-ascorbic acid: Myoglobin redox state, color and quality of refrigerated longtail tuna (Thunnus tonggol) slices.
Food Chem
February 2025
The International Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry Prince of Songkla University, Hat Yai, Songkhla 90110, Thailand; Department of Food and Nutrition, Kyung Hee University, Seoul 02447, Republic of Korea. Electronic address:
Effects of phenolic compounds in conjunction with L-cysteine/l-ascorbic acid on the redox state of myoglobin (Mb) and their efficacy to maintain the color and quality of refrigerated longtail tuna (Thunnus tonggol) slices were investigated. Purified metmyoglobin (metMb) and oxymyoglobin (oxyMb) samples were added with epigallocatechin-3-gallate (EGCG) or quercetin individually or in combination with L-cysteine (CT) or L-ascorbic acid (AA) at 4 °C. EGCG in combination with AA (EGCG+AA) and AA alone significantly reduced metMb and increased oxyMb levels (p < 0.
View Article and Find Full Text PDFDiscovery of Electrochemical Indicators upon Sarcoplasmic Meat Discoloration.
J Am Chem Soc
November 2024
Department of Chemistry, Oklahoma State University, Stillwater, Oklahoma 74078, United States.
Meat discoloration is one of the challenges facing the food industry, which affects both quality and shelf life. In this report, we present our groundbreaking discovery of electrochemically probing specific redox peaks associated with meat discoloration and successfully monitor its delay when controlled biochemically with added antioxidants. We have validated the redox features by spectrophotometry measurements of the relative levels of oxymyoglobin, which gives meat its cherry red color, and metmyoglobin, which causes the meat to turn brown in relation to discoloration.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!