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Subunit Mobility and the Chaperone Activity of Recombinant alphaB-Crystallin.

Krushelnitsky A, Mukhametshina N, Gogolev Y, Tarasova N, Faizullin D, Zinkevich T, Gnezdilov O, Fedotov V - Open Biochem J (2008)

Bottom Line: The comparison of the chaperone-like activity of native and covalently cross-linked human alphaB-crystallins has confirmed the important role of the subunit mobility in the chaperoning mechanism.Our data clearly demonstrate that the chaperone-like activity of alpha-crystallin is not only a surface phenomenon as was suggested by some researchers.

View Article: PubMed Central - PubMed

Affiliation: Kazan Institute of Biochemistry and Biophysics, Russian Academy of Sciences, Kazan, Russia.

ABSTRACT
The comparison of the chaperone-like activity of native and covalently cross-linked human alphaB-crystallins has confirmed the important role of the subunit mobility in the chaperoning mechanism. Our data clearly demonstrate that the chaperone-like activity of alpha-crystallin is not only a surface phenomenon as was suggested by some researchers.

No MeSH data available.


Aggregation kinetics of alcohol dehydrogenase (ADG) at 48 ºC. Alcohol dehydrogenase concentration was always 0.5 mg/ml, phosphate buffer, pH 7.0. Curves definition: 1 – pure ADG solution; 2 – ADG and native αB-crystallin at concentration 0.2 mg/ml; 3 – ADG and native αB-crystallin at concentration 0.05 mg/ml; 4 – ADG and cross-linked αB-crystallin at concentration 0.2 mg/ml; 5 – ADG and cross-linked αB-crystallin at concentration 0.05 mg/ml
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Figure 5: Aggregation kinetics of alcohol dehydrogenase (ADG) at 48 ºC. Alcohol dehydrogenase concentration was always 0.5 mg/ml, phosphate buffer, pH 7.0. Curves definition: 1 – pure ADG solution; 2 – ADG and native αB-crystallin at concentration 0.2 mg/ml; 3 – ADG and native αB-crystallin at concentration 0.05 mg/ml; 4 – ADG and cross-linked αB-crystallin at concentration 0.2 mg/ml; 5 – ADG and cross-linked αB-crystallin at concentration 0.05 mg/ml

Mentions: Figs. (4 and 5) present the measurements of the chaperone-like activity of αB-crystallin with hen egg white lysozyme and alcohol dehydrogenase as target proteins, respectively. It is clearly seen that the cross-linking essentially suppresses the αB-crystallin activity in comparison with the native αB-crystallin. These data are an indication of the essential role of the subunit mobility in the chaperoning mechanism of recombinant αB-crystallin and support many previous works on this topic cited in the Introduction. Thus, the chaperone activity is not always only a surface phenomenon as it is supposed in [17]. Our data nevertheless demonstrate that some surface effect does also exist since the cross-linked αB-crystallin sample reveals some activity as well.


Subunit Mobility and the Chaperone Activity of Recombinant alphaB-Crystallin.

Krushelnitsky A, Mukhametshina N, Gogolev Y, Tarasova N, Faizullin D, Zinkevich T, Gnezdilov O, Fedotov V - Open Biochem J (2008)

Aggregation kinetics of alcohol dehydrogenase (ADG) at 48 ºC. Alcohol dehydrogenase concentration was always 0.5 mg/ml, phosphate buffer, pH 7.0. Curves definition: 1 – pure ADG solution; 2 – ADG and native αB-crystallin at concentration 0.2 mg/ml; 3 – ADG and native αB-crystallin at concentration 0.05 mg/ml; 4 – ADG and cross-linked αB-crystallin at concentration 0.2 mg/ml; 5 – ADG and cross-linked αB-crystallin at concentration 0.05 mg/ml
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2570560&req=5

Figure 5: Aggregation kinetics of alcohol dehydrogenase (ADG) at 48 ºC. Alcohol dehydrogenase concentration was always 0.5 mg/ml, phosphate buffer, pH 7.0. Curves definition: 1 – pure ADG solution; 2 – ADG and native αB-crystallin at concentration 0.2 mg/ml; 3 – ADG and native αB-crystallin at concentration 0.05 mg/ml; 4 – ADG and cross-linked αB-crystallin at concentration 0.2 mg/ml; 5 – ADG and cross-linked αB-crystallin at concentration 0.05 mg/ml
Mentions: Figs. (4 and 5) present the measurements of the chaperone-like activity of αB-crystallin with hen egg white lysozyme and alcohol dehydrogenase as target proteins, respectively. It is clearly seen that the cross-linking essentially suppresses the αB-crystallin activity in comparison with the native αB-crystallin. These data are an indication of the essential role of the subunit mobility in the chaperoning mechanism of recombinant αB-crystallin and support many previous works on this topic cited in the Introduction. Thus, the chaperone activity is not always only a surface phenomenon as it is supposed in [17]. Our data nevertheless demonstrate that some surface effect does also exist since the cross-linked αB-crystallin sample reveals some activity as well.

Bottom Line: The comparison of the chaperone-like activity of native and covalently cross-linked human alphaB-crystallins has confirmed the important role of the subunit mobility in the chaperoning mechanism.Our data clearly demonstrate that the chaperone-like activity of alpha-crystallin is not only a surface phenomenon as was suggested by some researchers.

View Article: PubMed Central - PubMed

Affiliation: Kazan Institute of Biochemistry and Biophysics, Russian Academy of Sciences, Kazan, Russia.

ABSTRACT
The comparison of the chaperone-like activity of native and covalently cross-linked human alphaB-crystallins has confirmed the important role of the subunit mobility in the chaperoning mechanism. Our data clearly demonstrate that the chaperone-like activity of alpha-crystallin is not only a surface phenomenon as was suggested by some researchers.

No MeSH data available.