AI Article Synopsis
- The study examined how high pressure and high temperature affect glycation of a protein called ubiquitin using mass spectrometry.
- The researchers used glucose with stable isotopes to measure the extent of glycation under different conditions, finding that higher temperature led to more modifications compared to high pressure.
- They noted that pressures below 400 MPa showed minimal glycation changes, while pressures above 600 MPa had only a slight impact on glycation levels.
Article Abstract
The effect of high-pressure and/or high-temperature on the glycation of a model protein (ubiquitin) was investigated by mass spectrometry. This paper reports the impact of high pressure (up to 1200 MPa) on the modification of a ubiquitin using ESI-MS measurements. The application of glucose labeled with stable isotope allows a quantitative assessment of modification under the conditions of high-pressure (HPG) and high-temperature (HTG) glycation. A higher degree of modification was observed for the sample heated at 80 °C for 25 min under atmospheric pressure than for sample treated under high pressure. In samples treated at pressure below 400 MPa an insignificant increase of glycation level was observed, whereas high pressure (>600 MPa) has only a minor effect on the number of hexose moieties (Fru) attached to the lysine residue side chain.
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| http://dx.doi.org/10.1021/jf505628e | DOI Listing |
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