Thermal stability and aggregation of creatine kinase from rabbit skeletal muscle.

Maloletkina, Olga I.; Markossian, Kira A.; Belousova, L.V.; Kleimenov, S. Yu.; Орлов, В. Н.; Makeeva, Valentina F.; Bi, Kurganov

doi:10.1016/j.bpc.2010.03.005

Cited by 22 publications

(15 citation statements)

References 50 publications

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“…It should be noted that in some of our previous works (see, for example [3,41,42]) we used Equation (2) in the form: I = K LS ( t − t 2 ) 2 . The constant K LS in this equation has the following dimension: (counts/s) 1/2 ·min −1 .…”

Section: Methodsmentioning

confidence: 99%

Paradoxical Acceleration of Dithiothreitol-Induced Aggregation of Insulin in the Presence of a Chaperone

Bumagina

Gurvits

Artemova

et al. 2010

IJMS

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The kinetics of dithiothreitol (DTT)-induced aggregation of human recombinant insulin and the effect of α-crystallin, a representative of the family of small heat shock proteins, on the aggregation process have been studied using dynamic light scattering technique. Analysis of the distribution of the particles by size measured in the course of aggregation showed that the initial stage of the aggregation process was the stage of formation of the start aggregates with a hydrodynamic radius (Rh) of about 90 nm. When studying the effect of α-crystallin on the rate of DTT-induced aggregation of insulin, it was demonstrated that low concentrations of α-crystallin dramatically accelerated the aggregation process, whereas high concentrations of α-crystallin suppressed insulin aggregation. In the present study, at the molar stoichiometric ratio (insulin:α-crystallin) less than 1:0.5, a pronounced accelerating effect of α-crystallin was observed; whereas a ratio exceeding the value of 1:0.6 caused suppression of insulin aggregation. The mechanisms underlying the dual effect of α-crystallin have been proposed. It is assumed that heterogeneous nucleation occurring on the surface of the α-crystallin particle plays the key role in the paradoxical acceleration of insulin aggregation by α-crystallin that may provide an alternative biologically significant pathway of the aggregation process.

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Section: Methodsmentioning

confidence: 99%

Paradoxical Acceleration of Dithiothreitol-Induced Aggregation of Insulin in the Presence of a Chaperone

Bumagina

Gurvits

Artemova

et al. 2010

IJMS

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“…(3) for the description of the initial parts of the kinetic curves of protein aggregation was demonstrated for thermal denaturation of Ph b [50], [76], [78], [79], GAPDH [80]–[82] and creatine kinase (CK) [83]from rabbit skeletal muscles and DTT-induced aggregation of α-lactalbumin [18] and insulin [84]. The practical significance of Eqs.…”

Section: Theory Quantification Of the Chaperone-like Activitymentioning

confidence: 99%

Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

et al. 2013

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The methodology for quantification of the anti-aggregation activity of protein and chemical chaperones has been elaborated. The applicability of this methodology was demonstrated using a test-system based on dithiothreitol-induced aggregation of bovine serum albumin at 45°C as an example. Methods for calculating the initial rate of bovine serum albumin aggregation (v agg) have been discussed. The comparison of the dependences of v agg on concentrations of intact and cross-linked α-crystallin allowed us to make a conclusion that a non-linear character of the dependence of v agg on concentration of intact α-crystallin was due to the dynamic mobility of the quaternary structure of α-crystallin and polydispersity of the α-crystallin–target protein complexes. To characterize the anti-aggregation activity of the chemical chaperones (arginine, arginine ethyl ester, arginine amide and proline), the semi-saturation concentration [L]0.5 was used. Among the chemical chaperones studied, arginine ethyl ester and arginine amide reveal the highest anti-aggregation activity ([L]0.5 = 53 and 58 mM, respectively).

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“…Further sticking of the start aggregates and aggregates of higher order proceeds in the regime of what called "diffusion-limited cluster-cluster aggregation" (DLCA) as shown in Fig. 4c (Maloletkina et al, 2010). When this regime is fulfilled, the sticking probability for the colliding particles is equal to unity (Fig.…”

Section: Resultsmentioning

confidence: 92%

“…When this regime is fulfilled, the sticking probability for the colliding particles is equal to unity (Fig. 4d) (Maloletkina et al, 2010). DLS gives direct evidence for the thermal stability of HA lyase evaluated previously in which the enzyme had a significant activity in the temperature range 25-45 • C, then at 46 • C, the enzyme starts to lose most of its activity.…”

Section: Resultsmentioning

confidence: 94%

Characterization of hyaluronate lyase from Streptococcus pyogenes bacteriophage H4489A

El-Safory

Lee

2011

Carbohydrate Polymers

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Thermal stability and aggregation of creatine kinase from rabbit skeletal muscle.

Cited by 22 publications

References 50 publications

Paradoxical Acceleration of Dithiothreitol-Induced Aggregation of Insulin in the Presence of a Chaperone

Paradoxical Acceleration of Dithiothreitol-Induced Aggregation of Insulin in the Presence of a Chaperone

Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

Characterization of hyaluronate lyase from Streptococcus pyogenes bacteriophage H4489A

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