Effect of the Structure of the Denatured State of Lysozyme on the Aggregation Reaction at the Early Stages of Folding from the Reduced Form

Ohkuri, Takatoshi; Shioi, Seijiro; Imoto, Taiji; Ueda, Tadashi

doi:10.1016/j.jmb.2005.01.022

Cited by 29 publications

(33 citation statements)

References 28 publications

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“…We then evaluated the extent of the SS bond formation, as based on the ratio of the oxidized form to the reduced form of the protein, whereby each of these values was obtained from the peak area on the chromatographic pattern as in the our previous study. 12,14) The behavior of the SS bond formation on wild-type 1SSHEL was consistent with previous results. 12,14) Figure 3 shows the relative extent of SS bond formation on W111G and W123G 1SSHELs against that on wild-type 1SSHELs.…”

Section: Analyses Of Native Disulfide Bond Formations In the Earlysupporting

confidence: 92%

“…12,14) The behavior of the SS bond formation on wild-type 1SSHEL was consistent with previous results. 12,14) Figure 3 shows the relative extent of SS bond formation on W111G and W123G 1SSHELs against that on wild-type 1SSHELs. W111G mutation decreased the extent of formation of Cys30-Cys115 and Cys6-Cys127 whereas W123G mutation decreased only that of Cys6-Cys127 (Fig.…”

Section: Analyses Of Native Disulfide Bond Formations In the Earlysupporting

confidence: 92%

“…In order to examine the effects of disruptions of such long-range interactions on the folding process at the early stage, we measured the extent of SS bond formation among variants containing a pair of cysteines (1SS) in the wild-type and W62G HEL as a probe for the interactions involved in the formation of disulfide bonds at the early stages in the protein folding process. 12) A prominent interaction between cysteine residues seen in the wild-type protein disappeared in W62G 1SSHEL, suggesting that longrange interactions affect the formation of the disulfide bond. 12) On the other hand, Schwalbe's group and ours also have recently found that single-point mutations of the other hydrophobic residues modulated the compactness and long-range interactions of reduced HEL.…”

Section: Analyses Of Native Disulfide Bond Formations In the Earlymentioning

confidence: 99%

“…12) A prominent interaction between cysteine residues seen in the wild-type protein disappeared in W62G 1SSHEL, suggesting that longrange interactions affect the formation of the disulfide bond. 12) On the other hand, Schwalbe's group and ours also have recently found that single-point mutations of the other hydrophobic residues modulated the compactness and long-range interactions of reduced HEL.…”

Section: Analyses Of Native Disulfide Bond Formations In the Earlymentioning

confidence: 99%

“…15) According to previous methods, 12,14,16) the disulfide exchange equilibriums for four wild-type 1SSHELs, four W111G 1SSHELs, and four W123G 1SSHELs containing native disulfide bonds, Cys6-Cys127, Cys30-Cys115, Cys64-Cys80, or Cys76-Cys94, were performed in 0.1 M Tris-acetate containing 0.1 mM EDTA, pH 8.0, in the presence of 0.1 mM oxidized glutathione and 1 mM reduced glutathione with a protein concentration of 0.5 mM on incubation at 22 C for 4 h. The resulting equilibration products were analyzed by reverse-phase HPLC. Typical chromatograms for W111G and W123G Cys76-Cys94 HEL are shown in Fig.…”

Section: Analyses Of Native Disulfide Bond Formations In the Earlymentioning

confidence: 99%

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Analyses of Native Disulfide Bond Formations in the Early Stage of the Folding Process in Mutant Lysozymes Where the Long-Range Interactions in the Denatured State Were Modulated

Mishima

Ohkuri

Imoto

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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Section: Analyses Of Native Disulfide Bond Formations In the Earlysupporting

confidence: 92%

Section: Analyses Of Native Disulfide Bond Formations In the Earlysupporting

confidence: 92%

Section: Analyses Of Native Disulfide Bond Formations In the Earlymentioning

confidence: 99%

Section: Analyses Of Native Disulfide Bond Formations In the Earlymentioning

confidence: 99%

Section: Analyses Of Native Disulfide Bond Formations In the Earlymentioning

confidence: 99%

See 3 more Smart Citations

Analyses of Native Disulfide Bond Formations in the Early Stage of the Folding Process in Mutant Lysozymes Where the Long-Range Interactions in the Denatured State Were Modulated

Mishima

Ohkuri

Imoto

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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Indispensable structure of solution additives to prevent inactivation of lysozyme for heating and refolding

Matsuoka

Hamada

Matsumoto

et al. 2009

Biotechnology Progress

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This article investigates solution additives that prevent misfolding of lysozyme from heating treatment and during refolding processes. Comparison of heat treatment of native lysozyme and oxidative refolding from the reduced and denatured state of lysozyme in the presence of 44 different additives revealed an indispensable chemical structure for the additives to be effective against heat-induced misfolding and for refolding. The additives effective against heat treatment of native lysozyme possessed a main chain of the amino acid moiety. Amino acids that have esterificated and amidated carboxy groups prevented heat-induced misfoldings more effectively than amino acids themselves. On the other hand, the additives effective against oxidative refolding possessed a guanidium or ureido group. The former additives prevented hydrophobic interaction between the main chains of the unfolded polypeptide, while the latter additives increased the solubility of the aromatic and aliphatic side-chains. These data also support the fact that arginine (Arg) and Arg derivatives are versatile additives for both misfolding processes.

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Studies on Aggregation Interaction between Reduced‐Denatured Egg White Lysozymes during Refolding Procedure in Urea Solution

et al. 2007

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The aggregation interaction between reduced-denatured egg white lysozymes during refolding procedure in urea solution was studied by means of reducing and non-reducing protein electrophoreses. Results of non-reducing sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) of the supernatant and aggregate precipitate formed in refolding process show that except being refolded to native egg white lysozymes, the reduced-denatured lysozymes can also form the aggregates with molecular weights (MW) being separately about 30.0 and 35.0 kD, while the reducing SDS-PAGE and the refolding results in the presence of sodium dodecyl sulphate show that these aggregates are formed chiefly through the misconnection of disulfide bonds between the reduced-denatured lysozymes, and the aggregate precipitates are formed through the non-covalent interactions between the aggregates with molecular weight being about 30.0 kD. From the results of electrophoresis and size-exclusion chromatographic analyses, it can be inferred that the aggregates with molecular weights being about 30.0 and 35.0 kD are bi-molecular and tri-molecular egg white lysozyme aggregates, respectively. And finally, a suggested refolding mechanism of reduced-denatured egg white lysozymes in urea solution was presented.

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Effect of the Structure of the Denatured State of Lysozyme on the Aggregation Reaction at the Early Stages of Folding from the Reduced Form

Cited by 29 publications

References 28 publications

Analyses of Native Disulfide Bond Formations in the Early Stage of the Folding Process in Mutant Lysozymes Where the Long-Range Interactions in the Denatured State Were Modulated

Analyses of Native Disulfide Bond Formations in the Early Stage of the Folding Process in Mutant Lysozymes Where the Long-Range Interactions in the Denatured State Were Modulated

Indispensable structure of solution additives to prevent inactivation of lysozyme for heating and refolding

Studies on Aggregation Interaction between Reduced‐Denatured Egg White Lysozymes during Refolding Procedure in Urea Solution

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