Study of kinetics of thermal aggregation of mitochondrial aspartate aminotransferase by dynamic light scattering: protective effect of [alpha]-crystallin

Study of kinetics of thermal aggregation of mitochondrial aspartate aminotransferase by dynamic light scattering: protective effect of [alpha]-crystallin

Thermal aggregation of aspartate aminotransferase from pig heart mitochondria (mAAT) has been studied at various temperatures and various protein concentrations by dynamic light scattering. The character of the dependence of protein aggregate size on time indicates that aggregation of mAAT proceeds...

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Veröffentlicht in:European biophysics journal 2009-06, Vol.38 (5), p.547
Hauptverfasser: Golub, Nikolay V, Markossian, Kira A, Sholukh, Mikhail V, Muranov, Konstantin O, Kurganov, Boris I
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Heart
Hogs
Kinetics
Light scattering
Proteins
Studies
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container_issue 5
container_start_page 547
container_title European biophysics journal
container_volume 38
creator Golub, Nikolay V
Markossian, Kira A
Sholukh, Mikhail V
Muranov, Konstantin O
Kurganov, Boris I
description Thermal aggregation of aspartate aminotransferase from pig heart mitochondria (mAAT) has been studied at various temperatures and various protein concentrations by dynamic light scattering. The character of the dependence of protein aggregate size on time indicates that aggregation of mAAT proceeds in the regime of diffusion-limited cluster-cluster aggregation. Suppression of mAAT aggregation by α-crystallin is due to transition of the aggregation process into the regime of reaction-limited cluster-cluster aggregation. Realization of this regime of aggregation means that the sticking probability for the colliding particles is less than unity. (PUBLICATION ABSTRACT)
doi_str_mv 10.1007/s00249-009-0403-7
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subjects Heart
Hogs
Kinetics
Light scattering
Proteins
Studies
title Study of kinetics of thermal aggregation of mitochondrial aspartate aminotransferase by dynamic light scattering: protective effect of [alpha]-crystallin
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