Effect of α-crystallin on thermostability of mitochondrial aspartate aminotransferase

Markossian, Kira A.; Golub, Nikolay V.; Kleymenov, Sergey Y.; Muranov, Konstantin O.; Шолух, М. В.; Bi, Kurganov

doi:10.1016/j.ijbiomac.2009.03.006

Cited by 8 publications

(2 citation statements)

References 36 publications

(69 reference statements)

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“…Markossian, unpublished data). The analogous picture has been observed, when studying the effect of α-crystallin on thermal inactivation and denaturation of mAAT [ 127 ].…”

Section: Effect Of α-Crystallin On Thermal Stability Of Proteinssupporting

confidence: 69%

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Mechanism of Suppression of Protein Aggregation by α-Crystallin

Markossian

Yudin

2009

IJMS

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This review summarizes experimental data illuminating the mechanism of suppression of heat-induced protein aggregation by -crystallin, one of the small heat shock proteins. The dynamic light scattering data show that the initial stage of thermal aggregation of proteins is the formation of the initial aggregates involving hundreds of molecules of the denatured protein. Further sticking of the starting aggregates proceeds in a regime of diffusion-limited cluster-cluster aggregation. The protective effect of -crystallin is due to transition of the aggregation process to the regime of reaction-limited cluster-cluster aggregation, wherein the sticking probability for the colliding particles becomes lower than unity.

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“…Markossian, unpublished data). The analogous picture has been observed, when studying the effect of α-crystallin on thermal inactivation and denaturation of mAAT [ 127 ].…”

Section: Effect Of α-Crystallin On Thermal Stability Of Proteinssupporting

confidence: 69%

“…The effect of α-crystallin on the thermostability of mAAT characterized by DSC is shown in Figure 19 [ 127 ]. The DSC profile for mAAT (1 mg/mL) has a maximum ( T max ) of 72.4 °C (curve 1).…”

Section: Effect Of α-Crystallin On Thermal Stability Of Proteinsmentioning

confidence: 99%

Mechanism of Suppression of Protein Aggregation by α-Crystallin

Markossian

Yudin

2009

IJMS

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Comparative Analysis of the Effects of α-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase

et al. 2009

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Effects of alpha-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH) have been studied using dynamic light scattering and analytical ultracentrifugation. The analysis of the initial parts of the dependences of the hydrodynamic radius of protein aggregates on time shows that in the presence of alpha-crystallin or GroEL the kinetic regime of GAPDH aggregation is changed from the regime of diffusion-limited cluster-cluster aggregation to the regime of reaction-limited cluster-cluster aggregation, wherein the sticking probability for the colliding particles becomes lower the unity. In contrast to alpha-crystallin, GroEL does not interfere with formation of the start aggregates which include denatured GAPDH molecules. On the basis of the analytical ultracentrifugation data the conclusion has been made that the products of dissociation of GAPDH and alpha-crystallin or GroEL play an important role in the interactions of GAPDH and chaperones at elevated temperatures.

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