Two-state irreversible thermal denaturation of Euphorbia characias latex amine oxidase

Amani, Mojtaba; Moosavi-Movahedi, Ali Akbar; Floris, Giovanni; Mura, Anna; Bi, Kurganov; Ahmad, Faizan; Saboury, Ali Akbar

doi:10.1016/j.bpc.2006.08.006

Cited by 17 publications

(12 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The reversibility of protein refolding depends on various conditions such as the nature of the protein, heating rate, cooling rate and the maximum temperature in the first scan [38]. When lysozyme was heated up to 80 • C, its denaturation was reversible.…”

Section: Resultsmentioning

confidence: 99%

“…If the original curve completely or partially reproduced, it is evident that denaturation is fully or partially reversible; otherwise it is an irreversible process. The extent of reversibility depends on a number of factors including temperature to which the protein was heated in the first scan [38].…”

Section: Calorimetric Studiesmentioning

confidence: 99%

“…For this purpose, we measured the stability and aggregation rate of lysozyme using different methods including differential scanning calorimetry (DSC). DSC is widely used for the study of thermal protein denaturation, and is the sole method for direct determination of the thermodynamic parameters of proteins [35][36][37][38][39]. Here we demonstrate how ␤-casein with negative charge on its surface can change its chaperone activity toward a target protein with positive charge.…”

Section: Introductionmentioning

confidence: 95%

See 2 more Smart Citations

Acidic residue modifications restore chaperone activity of β-casein interacting with lysozyme

Moosavi-Movahedi

Rajabzadeh

Amani

et al. 2011

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 99%

Section: Calorimetric Studiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 95%

See 1 more Smart Citation

Acidic residue modifications restore chaperone activity of β-casein interacting with lysozyme

Moosavi-Movahedi

Rajabzadeh

Amani

et al. 2011

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

“…Recently, a vast number of cysteine proteases have been described as occurring in many latex-producing plants (Liggieri et al 2004;Morcelle et al 2004a, b). Chitinases, lectins, lipases, oxidative and other hydrolytic enzymes have also been described as occurring in latex fluids (Stirpe et al 1993;Azarkan et al 1997;Giordani et al 1992;Amani et al 2007;Fiorillo et al 2007). These findings on the biochemical composition of laticifer fluids support the hypothesis of their defensive role (Taira et al 2005).…”

Section: Introductionmentioning

confidence: 98%

The defensive role of latex in plants: detrimental effects on insects

Ramos

Grangeiro

Freire

et al. 2010

Arthropod-Plant Interactions

View full text Add to dashboard Cite

The defensive role of the latex of Calotropis procera has recently been reported. In this study, latex proteins involved in detrimental effects on insects were evaluated on another important crop pest. The latex was fractionated to obtain its major protein fraction, which was then used to evaluate its insecticidal properties against Callosobruchus maculatus (Coleoptera: Bruchidae) in artificial bioassays. Laticifer proteins (LP) were investigated to characterize their action in such an activity. LP was highly insecticidal at doses as low as 0.1% (W/W). This effect was slightly augmented in F 1 generation reared in artificial seeds containing LP at similar proportions of F 0 , but was fully reversed when F 1 developed in LP-free seeds. The insecticidal proteins were not retained in a chitin column, and did not lose their insecticidal activity, even after heat treatment or pronase digestion. However, these samples inhibited papain (EC 3.4.22.2) activity and gut proteases of C. maculatus larvae, and a reverse zymogram showed the presence of protein bands resistant to papain digestion. These activities were not observed in unheated LP as they were probably masked by abundant endogenous cysteine protease (EC 3.4.22.16) activity present in unheated LP. LP was resistant to proteolysis when assayed with C. maculatus gut extract. However, gut proteins of C. maculatus were digested when incubated with LP. These observations and the deleterious effects of LP upon C. maculatus, reinforce the hypothesis that laticifer fluids are involved in plant defense against insects and indicate C. procera latex to be a source of promising insecticidal proteins. The inhibitor of proteolysis present in the latex seems to be resistant to heat and proteolysis and is certainly involved in the detrimental effects observed.

show abstract

“…Numerical data analysis of the THI1 and THI1(A140V) thermal unfolding process was based on the two-state Lumry-Eyring model of unfolding [29,30]. The ellipticity measured by CD spectroscopy was analyzed assuming that this is an irreversible two-state process:…”

Section: Data Analysesmentioning

confidence: 99%

THI1, a protein involved in the biosynthesis of thiamin in Arabidopsis thaliana: Structural analysis of THI1(A140V) mutant

Garcia

Dyszy

Munte

et al. 2014

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

View full text Add to dashboard Cite

Two-state irreversible thermal denaturation of Euphorbia characias latex amine oxidase

Cited by 17 publications

References 22 publications

Acidic residue modifications restore chaperone activity of β-casein interacting with lysozyme

Acidic residue modifications restore chaperone activity of β-casein interacting with lysozyme

The defensive role of latex in plants: detrimental effects on insects

THI1, a protein involved in the biosynthesis of thiamin in Arabidopsis thaliana: Structural analysis of THI1(A140V) mutant

Contact Info

Product

Resources

About