Radiation Damage to Proteins

Kumta, U.S.; Tappel, Al L.

doi:10.1038/1911304a0

Cited by 35 publications

(15 citation statements)

References 6 publications

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“…Since radiation is known to cause disintegration and aggregation of protein molecule this may be occur in the present investigation (Kumta and Tappel, 1961), which will effect on the protein solubility. While it is known that gamma radiation is generally attributed to direct breakdown in protein or enhance the activity of lysozomal (proteolytic) enzyme, which help to aggregate the protein and decrease its solubility (Van Huystee and Verma, 1969).…”

Section: Soybean Protein Profilesmentioning

confidence: 99%

Effect of Gamma Radiation on Protein Profile, Protein Fraction and Solubility’s of Three Oil Seeds: Soybean, Peanut and Sesame

Afify

Rashed

Mahmoud

et al. 2011

Not Bot Hort Agrobot Cluj

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The proteins properties of three oil seeds (soybean, peanut and sesame) were investigated following γ-irradiation (0.0, 0.5, 1.0, 2.0, 3.0, 5.0 and 7.5 KGy). The effect of γ-radiation on total protein solubility, albumin, globulin and SDS-ME fractions were studied using SDS-polyacrylamide gel electrophoresis. The results showed that solubility of total protein were decreased and reached to the maximum decrease using irradiation dose of 7.5 KGy compared to control. The interesting phenomena are that albumin and globulin fractions decreased in its solubility while the SDS-ME fraction increased. These phenomena may be due to the effect of gamma radiation on the protein, which may dissociate this fraction to small subunits, and rearrangement to form a complex protein even high or small molecular weight proteins solubilized only in SDS-ME fraction. The changes in protein profile were depended even on radiation dose and on the nature of oil seeds; soybean, peanut and sesame.

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Section: Soybean Protein Profilesmentioning

confidence: 99%

Effect of Gamma Radiation on Protein Profile, Protein Fraction and Solubility’s of Three Oil Seeds: Soybean, Peanut and Sesame

Afify

Rashed

Mahmoud

et al. 2011

Not Bot Hort Agrobot Cluj

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“…Proteins damaged by ROS were found to be rapidly degraded in RBC lysates as oxidation increases their susceptibility to intracellular proteases . Moreover, oxidative protein–protein cross‐linking can cause the formation of insoluble protein aggregates . It can be assumed, that the altered proteins were sensitive to oxidative damage due to certain structural characteristics or an exposed cellular localization.…”

Section: Resultsmentioning

confidence: 99%

Effects of gamma irradiation and 15 days of subsequent ex vivo storage on the cytosolic red blood cell proteome analyzed by 2D‐DIGE and Orbitrap MS

Walpurgis

Kohler

Thomas

et al. 2013

Proteomics Clinical Apps

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“…In addition, this treatment decreased protein solubility, as observed for the albumin and globulin fractions of certain oil seeds (soybean, peanut and sesame) [ 45 , 46 ]. Furthermore, it is possible that radiation causes protein fragmentation and aggregation, with the latter effect leading to protein insolubility [ 47 , 48 ]. A protein-free (NPC) diet and an EW-based diet were used as controls.…”

Section: Discussionmentioning

confidence: 99%

Increased Levels of Antinutritional and/or Defense Proteins Reduced the Protein Quality of a Disease-Resistant Soybean Cultivar

et al. 2015

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The biochemical and nutritional attributes of two soybean (Glycine max (L.) Merr.) cultivars, one susceptible (Seridó) and the other resistant (Seridó-RCH) to stem canker, were examined to assess whether the resistance to pathogens was related to levels of antinutritional and/or defense proteins in the plant and subsequently affected the nutritional quality. Lectin, urease, trypsin inhibitor, peroxidase and chitinase activities were higher in the resistant cultivar. Growing rats were fed with isocaloric and isoproteic diets prepared with defatted raw soybean meals. Those on the Seridó-RCH diet showed the worst performance in terms of protein quality indicators. Based on regression analysis, lectin, trypsin inhibitor, peroxidase and chitinase appear to be involved in the resistance trait but also in the poorer nutritional quality of Seridó-RCH. Thus, the development of cultivars for disease resistance may lead to higher concentrations of antinutritional compounds, affecting the quality of soybean seeds. Further research that includes the assessment of more cultivars/genotypes is needed.

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Radiation Damage to Proteins

Cited by 35 publications

References 6 publications

Effect of Gamma Radiation on Protein Profile, Protein Fraction and Solubility’s of Three Oil Seeds: Soybean, Peanut and Sesame

Effect of Gamma Radiation on Protein Profile, Protein Fraction and Solubility’s of Three Oil Seeds: Soybean, Peanut and Sesame

Effects of gamma irradiation and 15 days of subsequent ex vivo storage on the cytosolic red blood cell proteome analyzed by 2D‐DIGE and Orbitrap MS

Increased Levels of Antinutritional and/or Defense Proteins Reduced the Protein Quality of a Disease-Resistant Soybean Cultivar

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