Mass spectrometric investigations on lactate adduction to equine myoglobin.
Abstract: Research focused on determining the fundamental mechanisms by which lactate influences color stability has not considered a direct effect of lactate on myoglobin. Thus, the objective of this study was to use Matrix Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry to examine lactate adduction to myoglobin. Equine oxymyoglobin and equine carboxymyoglobin (0.15mM) were incubated with sodium lactate (200mM) at 4 degrees C, pH 5.6 in 50mM sodium citrate buffer or at 37 degrees C, pH 7.4 in 50mM sodium phosphate buffer, simulating typical meat storage and physiological conditions, respectively. Controls consisted of myoglobin plus a volume of deionized water equivalent to that used to deliver the lactate treatments. No peaks corresponding to lactate-Mb adducts could be detected in the mass spectra of samples incubated up to 360min at pH 7.4, 37 degrees C or 8days at pH 5.6 and 4 degrees C. Our results suggest that lactate did not form covalent adducts with equine oxy- and carboxy-myoglobin.
Copyright 2010 Elsevier Ltd. All rights reserved.
Publication Date: 2010-02-08 PubMed ID: 20374912DOI: 10.1016/j.meatsci.2010.02.006Google Scholar: Lookup
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- Journal Article
Summary
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This paper investigates whether lactate, a molecule produced during physical exertion, interacts directly with myoglobin, a protein in muscle tissue, using laser-based investigative techniques. The study found that there is presumably no direct interaction between the lactate and the myoglobin.
Research Methodology
- The researchers targeted their investigation on lactate’s direct effect on myoglobin. Myoglobin is a protein found in muscle cells and is responsible for transporting oxygen within these cells. Lactate is a chemical compound formed in the body through the process of anaerobic respiration and is often associated with muscle fatigue during strenuous physical activities.
- Two types of myoglobin were used for this study: equine oxymyoglobin and equine carboxymyoglobin, at a concentration of 0.15 millimolar.
- The myoglobins were incubated with sodium lactate (200mM) under two different conditions: at a cold temperature of 4 degrees Celsius, pH 5.6, in 50mM sodium citrate buffer to mimic meat storage conditions, and at body temperature (37 degrees Celsius), pH 7.4, in 50mM sodium phosphate buffer to mimic physiological conditions.
- Control variables involved myoglobin and an equivalent volume of deionized water used to introduce lactate.
Research Findings
- The team utilized a technique called Matrix Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry (MALDI-ToF MS) to observe any interactions between the lactate and myoglobin. This technique permits the identification and characterization of biological compounds like proteins and peptides.
- They analyzed the samples after incubation at different intervals up to 360 minutes at body temperature and up to 8 days at cold storage temperature. They were examining for peaks in the mass spectra which would symbolize lactate-myoglobin adducts—evidence of a chemical bond formation between lactate and myoglobin.
- No such “lactate-Mb adducts” were noted. Hence, the research suggests that there is no direct chemical interaction between lactate and both types of myoglobin under the conditions tested.
Cite This Article
APA
Mancini RA, Suman SP, Konda MK, Ramanathan R, Joseph P, Beach CM.
(2010).
Mass spectrometric investigations on lactate adduction to equine myoglobin.
Meat Sci, 85(2), 363-367.
https://doi.org/10.1016/j.meatsci.2010.02.006 Publication
Researcher Affiliations
- Department of Animal Science, University of Connecticut, Storrs, CT 06269, USA.
MeSH Terms
- Animals
- Color
- Horses
- Lactates / chemistry
- Myoglobin / chemistry
- Oxidation-Reduction
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Citations
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