A deuteron and proton magnetic resonance relaxation study of β-lactoglobulin A association: Some approaches to the scatchard hydration of globular proteins

Kumosinski, Thomas F.; Pessen, Helmut

doi:10.1016/0003-9861(82)90347-2

Cited by 42 publications

(42 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The obtained relaxation times for BLG were in the range from 1918 to 2143 ms, which is similar to the values obtained by Indrawati, Stroshine, and Narsimhan (2007) and Kumosinski and Pessen (1982) for similar concentrations of BLG. A significantly shorter T 2 relaxation time was obtained for the BSM, indicating a stronger protein-water interaction and more "restricted" water structure in the BSM solutions compared to the BLG solutions.…”

Section: T 2 Relaxation Time Assignment By Low Field Nmrsupporting

confidence: 82%

Spectroscopic studies of the interactions between β-lactoglobulin and bovine submaxillary mucin

et al. 2015

View full text Add to dashboard Cite

Section: T 2 Relaxation Time Assignment By Low Field Nmrsupporting

confidence: 82%

Spectroscopic studies of the interactions between β-lactoglobulin and bovine submaxillary mucin

et al. 2015

View full text Add to dashboard Cite

“…The decrease in the T2/ T1 ratio observed for the apoovotransferrin aqueous solution ( Figure 2) indicates that cross-relaxation does not make a major contribution to relaxation in the protein concentration range 2-10%. This is confirmed (Kumosinski and Pessen, 1982) by the longitudinal ( T I ) relaxation of water protons being a single exponential in apoovotransferrin aqueous solutions. The gradual decrease in the T2/ T I ratio as a function of the protein concentration ( Figure 2) might reflect an exchange between water proton and protein proton (Myers-Betts and Baianu, 1990a).…”

Section: Resultssupporting

confidence: 72%

“…This indicates that the protein activity is small in this concentration range and does not contribute to the 'H relaxation rates (Kumosinski and Pessen, 1982;MyersBetts and Baianu, 1990b).…”

Section: Resultsmentioning

confidence: 91%

Low-field nuclear magnetic resonance relaxation study of the thermal denaturation of transferrins

Lambelet¹,

Ducret²,

Leuba³

et al. 1991

J. Agric. Food Chem.

View full text Add to dashboard Cite

The NMR method previously described by Lambelet et al. (J. Dairy Res. 1989,56,211-222) has been evaluated for the investigation of thermal and acid denaturation of transferrins in aqueous solution.Heating an apoovotransferrin or an apolactoferrin solution resulted in a slight increase in T1-l and an important increase in T2-1 relaxation rates within the denaturation range. The same treatment applied to corresponding iron-saturated proteins resulted in a decrease in these parameters due to modifications of the metal-protein complex accompanying the denaturation. It is proposed that these changes in NMR relaxation parameters can be used to monitor thermal denaturation of transferrins. Acid treatment led to a decrease in relaxation parameters for both apoovotransferrin and iron-saturated (down to pH 4) ovotransferrin. These variations in NMR parameters were related to protein denaturation and indicated that the protein modifications due to acid treatment were different from those occurring during heating.

show abstract

“…From a macroscopic point of view, it can be assumBd that a three-component system like salt/protein/water is a complex mixture of free salt, salt interacting with the protein and free protein. The basis of this hypothesis has been discussed, for dilute solutions, by Kumosinski and Pessen (1982). The difficulties encountered with powdered proteins have led Lang and Steinberg (1980) and Hardy and Steinberg (1984) to develop an equation which allows the prediction of the amount of salt.…”

Section: Gravimetric Interacting Salt Determinationmentioning

confidence: 99%

¹H and ²³Na NMR Relaxation Studies of the NaCl/β‐Lactoglobulin System Equilibrated at Various Water Activities

Fanni¹,

Canet²,

Elbayed³

et al. 1989

Journal of Food Science

View full text Add to dashboard Cite

NMR relaxation times (T,) of 'H and 2"Na were determined at 8, 14, 60, MHz and at 14,52 MHz, respectively, in the NaCI/@lactoglobulin system equilibrated at water activities ranging from 0.11 to 0.97. A two-state model was used for both nuclei which allowed the calculation of proportions of bound and free species. It was shown that bound water and Na+ increased at medium water activities in the presence of increasing NaCI. The discrepancy with adsorption isotherms data was explained by (1) limitations of the mass balance equation used to calculate interacting salt by gravimetry and (2) the fact that NMR probed the totality of ions in the vicinity of the protein, whereas adsorption isotherms were indicative of sodium choride tightly bound to the protein. It was also shown that the protein and Na' shared available water molecules at medium and low water activity.

show abstract

A deuteron and proton magnetic resonance relaxation study of β-lactoglobulin A association: Some approaches to the scatchard hydration of globular proteins

Cited by 42 publications

References 40 publications

Spectroscopic studies of the interactions between β-lactoglobulin and bovine submaxillary mucin

Spectroscopic studies of the interactions between β-lactoglobulin and bovine submaxillary mucin

Low-field nuclear magnetic resonance relaxation study of the thermal denaturation of transferrins

¹H and ²³Na NMR Relaxation Studies of the NaCl/β‐Lactoglobulin System Equilibrated at Various Water Activities

Contact Info

Product

Resources

About

A deuteron and proton magnetic resonance relaxation study of β-lactoglobulin A association: Some approaches to the scatchard hydration of globular proteins

Cited by 42 publications

References 40 publications

Spectroscopic studies of the interactions between β-lactoglobulin and bovine submaxillary mucin

Spectroscopic studies of the interactions between β-lactoglobulin and bovine submaxillary mucin

Low-field nuclear magnetic resonance relaxation study of the thermal denaturation of transferrins

1H and 23Na NMR Relaxation Studies of the NaCl/β‐Lactoglobulin System Equilibrated at Various Water Activities

Contact Info

Product

Resources

About

¹H and ²³Na NMR Relaxation Studies of the NaCl/β‐Lactoglobulin System Equilibrated at Various Water Activities