Conformational stability and dissociation of a peanut storage protein (arachin) exposed to organic solvents

Jacks, T. J.; Hensarling, T. P.; Neucere, Navin J.; Graves, Elena

doi:10.1021/jf00115a003

Cited by 6 publications

(4 citation statements)

References 6 publications

(11 reference statements)

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“…The data indicate that the microenvironment around the various chromophores in arachin is not perturbed, and the secondary structure of arachin is unchanged even at 150 mM citrate concentrations. These results are in excellent agreement with those of Jacks et al (14), who have shown that the dissociation of arachin did not change the secondary structure of the multimer in acidic hexane.…”

Section: Resultssupporting

confidence: 92%

Modification of arachin‐effect of citrate ions‐structural implications

Prakash

Rao

1987

J Americ Oil Chem Soc

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The effect of the anion citrate on the subunit structure of arachin has been monitored by velocity sedimentation, viscosity and circular dichroism techniques. The results indicate that as the concentration of citrate ion increases from 25 mM to 150 raM, arachin dissociates progressively to the low molecular weight 2S component. This dissociation is not accompanied by any conformational changes or denaturation as revealed by the far ultraviolet circular dichroic spectra and viscosity results, respectively. The results are explained by direct anion binding and changes in the solvent structure.

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Section: Resultssupporting

confidence: 92%

Modification of arachin‐effect of citrate ions‐structural implications

Prakash

Rao

1987

J Americ Oil Chem Soc

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“…For comparison, arachin (principal storage protein of the peanut) showed increased content of unordered structure when heated above 140 °C from circular dichroism measurement (Jacks et al, 1975). On the other hand, arachin maintained the native secondary structure of the multimeric form after irreversible dissociation by acidic hexane into subunits (Jacks et al, 1983).…”

Section: Resultsmentioning

confidence: 99%

Conformation of Bowman-Birk Inhibitor

Wu¹,

Sessa²

1994

J. Agric. Food Chem.

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Bowman-Birk inhibitor, a major trypsin and chymotrypsin inhibitor from soybean, has 71 amino acids with 7 disulfide bonds. Conformation of Bowman-Birk inhibitor in native state, after heating, and after disulfide bonds were broken by sodium metabisulfite was determined by circular dichroism.The native Bowman-Birk inhibitor has 61% /3-sheet, 38% unordered form, 1% /3-turn, and no -helical structure. There was no significant change in conformation after Bowman-Birk inhibitor was heated at 80 °C for 1 h in phosphate buffer. There was a decrease in /3-sheet and an increase in /3-turn structure after Bowman-Birk inhibitor was heated at 80 °C for 1 h in sodium metabisulfite-phosphate buffer. Although the change in conformation after disulfide bonds of Bowman-Birk inhibitor were broken was statistically significant (P < 0.05), the magnitude of the change was not large. The data support Bowman-Birk inhibitor's having a stable conformation even after disulfide bonds are broken.

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“…SDS-gel electrophoresis (figure not shown), however, showed no difference either in the mobility or in the intensity of bands among different isolates. Jacks et al (1983) have reported that arachin exposed to acidic hexane resulted in dissociation as evidenced by increased mobility in nondenaturing gels but no corresponding change of migrational pattern in dissociating sodium dodecyl sulfate gels.…”

Section: Yield Of Protein Isolates and Their Qualitymentioning

confidence: 99%