Symposium Discussion

Henderson, Madeline M.

doi:10.1021/c160031a017

Cited by 3 publications

(3 citation statements)

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“…It was found that T p at pH 7.0 is approximately 3°C higher in D 2 O compared to H 2 O; at pH 6.5 this difference in T p is somewhat less (2.6°C). Thus, the DSC measurements show a significantly increased conformational stability of the protein in D 2 O over that in H 2 O, as was already found for some other proteins [1–8]. Addition of 0.1 M NaCl to the medium increased T p by 0.5–0.8°C at both pH values in D 2 O and H 2 O.…”

Section: Resultssupporting

confidence: 81%

“…In order to determine whether replacement of H 2 O with D 2 O influences the mechanism by which the heat‐induced denaturation and aggregation of β‐lg takes place, a comparative study was undertaken. Previous studies already revealed that the conformational stability of some proteins increases in D 2 O over that in H 2 O [1–8]. This stabilizing effect of D 2 O was explained by an increase in hydrophobic interactions and/or an isotope effect on hydrogen bonding [3, 5, 6].…”

Section: Introductionmentioning

confidence: 96%

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Aggregation of β‐lactoglobulin and influence of D₂O

1998

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The conformational stability of L L-lactoglobulin increases in D P O over that in H P O. This is concluded from an increase in peak temperature by about 3³C of differential scanning calorimetry (DSC) thermograms and from a decrease in overall aggregation rate. However, effects of pH and salt concentration on the heat-induced aggregation (reaction kinetics, DSC thermograms and aggregate growth) are similar in H P O and D P O. This indicates that the mechanism of heat-induced aggregation of L L-lactoglobulin is not significantly affected by replacement of H P O with D P O.z 1998 Federation of European Biochemical Societies.

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