Diminishing of aggregation for bovine liver catalase through acidic residues modification

Hashemnia, Sedigheh; Moosavi-Movahedi, Ali Akbar; Ghourchian, Hedayatollah; Ahmad, Faizan; Hakimelahi, G. H.; Saboury, Ali Akbar

doi:10.1016/j.ijbiomac.2006.05.011

Cited by 24 publications

(15 citation statements)

References 53 publications

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“…Reversal of charge, and providing new opportunities for hydrogen bonding with the modified group attached to lysine residues could be suggested to have a role in this regard [51]. Modification could also diminish surface hydrophobicity without affecting net charge, and lower the aggregation propensity of the protein [119]. In the same line of studies, the effect of homobifunctional cross-linkers providing intramolecular cross links between lysine residues was also investigated on thermal stabilization of this enzyme as also observed for a number of other proteins [120,121].…”

Section: Chemical Modificationmentioning

confidence: 99%

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

Ebrahim‐Habibi

Morshedi

Rezaei‐Ghaleh

et al. 2010

JICS

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Protein aggregates, whether amorphous or structured (amyloid), have attracted much attention in recent years and despite extensive efforts, the mechanism of their formation is poorly understood. While "natural" aggregation (polymerization) of monomers could improve the biological function of some proteins, it is usually the darker side of this phenomenon which is discussed in many studies: deleterious aggregation that could lead to loss of biological activity under in vitro conditions or cause misfolding diseases. In this review, protein aggregation has been overviewed, starting from some general concepts involved in its formation, followed by mentioning studies aimed at elucidation of its kinetics and mechanism, or characterization of intermediates that would be aggregation-prone, and finally, reporting some of the studies related to the design of methods that would control the process. Similarly, amyloid aggregates have been defined, and current methods used in their characterization have been briefly described, with an emphasis on in silico studies. Finally, identification and design of such molecules which may be effective in control of this process is discussed.

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Section: Chemical Modificationmentioning

confidence: 99%

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

Ebrahim‐Habibi

Morshedi

Rezaei‐Ghaleh

et al. 2010

JICS

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“…The concentration of Ct stock solution was determined by measurement of its absorbance at 405 nm, using 3.24 9 10 5 M -1 cm -1 for the molar extinction coefficient [33] and 250,000 Daltons for the molecular mass of the enzyme. Selective modification of exposed carboxylate groups of Ct (0.5 mg mL -1 ) was carried out with WRK (10 mM) using the procedure described in our previous work [24].…”

Section: Chemical Modification Of Catalasementioning

confidence: 99%

“…Such a separation of the activation step from nucleophilic displacement allows one to choose conditions which are optimal for each step. This situation is not possible in the procedure with water-soluble carbodiimide, since the activation and displacement steps must be carried out simultaneously [24][25][26].…”

Section: Introductionmentioning

confidence: 99%

Direct electrochemistry of chemically modified catalase immobilized on an oxidatively activated glassy carbon electrode

et al. 2008

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Catalase (Ct) was modified using Woodward's reagent K (WRK) as a specific modifier of carboxyl residues. The modified Ct was immobilized on an oxidatively activated glassy carbon electrode surface to investigate its direct electrochemistry. Using cyclic voltammetry an irreversible reduction peak was obtained at approximately -0.362 V vs. Ag/AgCl in buffer solution, pH 7, and at a scan rate of 0.1 V s -1 . The electrochemical parameters, including charge-transfer coefficient (0.27), apparent heterogeneous electron transfer rate constant (13.51 ± 0.42 s -1 ) and formal potential of the Ct film (-0.275 V) were determined. The prepared enzyme electrode exhibited a response to H 2 O 2 .

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“…The aggregation of IP-10 could be prevented by reduction of its sulfhydryls with dithiothreitol followed by irreversible blockade with iodoacetamide (Crow et al, 2001). Moreover, the chemical modification of carboxyl residues by MIA cause the conformational change of the protein at the tertiary level, so that it conceals hydrophobic residues and reduces the proteinprotein interaction due to loss in hydrophobicity and also reduces the aggregation of protein (Hashemnia et al, 2006) (Pighin et al, 2008). Such condition also increases the ionic repulsion which decreases the protein-protein as well as the inter polypeptides interaction.…”

Section: Discussionmentioning

confidence: 99%

Thermally induced aggregation and its suppression of silkworm small heat shock protein sHSP19.9

Hossain

Aso

2017

Bang. J. Anim. Sci.

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About ten genes responsible for small heat-shock proteins (sHSP) have been isolated from silkworm. sHSP19.9 is one of the important member among them. Heat-induced stability of the sHSP was investigated at 60ºC with 20 mM HEPES buffer pH 7.7 containing 10 mM NaCl (low-ionic strength).Along with it probable suppression of the aggregation was also examined. At the mentioned reaction medium, sHSP19.9 was observed to be aggregated on the concentration-and time-dependent manners.It was successfully suppressed with dithiothreitol (DTT), higher-ionic strengths, Cysteine residues modifications and molecular chaperone: sHSP20.8.

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Diminishing of aggregation for bovine liver catalase through acidic residues modification

Cited by 24 publications

References 53 publications

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

Direct electrochemistry of chemically modified catalase immobilized on an oxidatively activated glassy carbon electrode

Thermally induced aggregation and its suppression of silkworm small heat shock protein sHSP19.9

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