A Critical Analysis of the Use of Radiation Inactivation to Measure the Mass of Protein

Lidzey, David G.; Berovic, N.; Chittock, Roger S.; Beynon, T.D.; Wharton, Christopher W.; Jackson, John L.; Parkinson, N.S.

doi:10.2307/3579155

Cited by 11 publications

(7 citation statements)

References 7 publications

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“…While one may (and perhaps should) question the accuracy of target size estimation by radiation inactivation of non-globular membrane proteins [24], there are also some interesting results from radiation inactivation studies that are less dependent on the exact size determination. Two laboratories reported that the formation of diglucuronide conjugates of either bilirubin [27] or 3,6-dihydroxybenzo(a)pyrene [25] required significantly larger protein complexes than the formation of the respective mono-glucuronides.…”

Section: Monomers Dimers or Higher Oligomers?mentioning

confidence: 97%

“…In optimal cases, radiation inactivation analyses might reveal considerable information on the size and quaternary structure of the enzyme [23]. In reality, however, the results are often less clear and may vary significantly between different proteins [24]. In the case of UGTs, some of the target sizes that were estimated, such as 91 ± 29 kDa [25] or 95 ± 18 [26], could agree with either monomeric or dimeric enzymes.…”

Section: Monomers Dimers or Higher Oligomers?mentioning

confidence: 99%

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The UDP-Glucuronosyltransferases as Oligomeric Enzymes

Finel¹,

Kurkela

2008

CDM

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The UDP-glucuronosyltransferases (UGTs) are integral membrane proteins of the endoplasmic reticulum that play important roles in the defense against potentially hazardous xenobiotics. The UGTs also participate in the metabolism and homeostasis of many endogenous compounds, including bilirubin and steroid hormones. Most human UGTs can glucuronidate several substrates the chemical structures of which may vary significantly. Understanding the structural basis for the complex substrate specificity of the UGTs is a major challenge that is hampered by the lack of sufficient structural information on these enzymes. Nevertheless, there is currently a broad interest in the structure and function of the UGTs and here we have focused on their oligomeric state. The question whether or not the UGTs are oligomeric enzymes, either dimeric or tetrameric, was frequently addressed in the past, as well as in recent studies. The current knowledge of protein-protein interactions among the UGTs is limited, however, primarily due to considerable difficulties in purifying individual recombinant UGTs as fully active and mono-dispersed proteins. Such hurdles in studying the oligomeric state of the UGTs prompted researchers to develop less direct approaches for examining the quaternary structure of the UGTs and its functional significance. In this article we have reviewed, sometimes critically, most of the available studies about the oligomeric state of the UGTs. Concluding that the UGTs are oligomeric enzymes, we discuss hetero-oligomerization among UGTs and its possible implications for the structure, function and substrate specificity of the enzymes.

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Section: Monomers Dimers or Higher Oligomers?mentioning

confidence: 97%

Section: Monomers Dimers or Higher Oligomers?mentioning

confidence: 99%

The UDP-Glucuronosyltransferases as Oligomeric Enzymes

Finel¹,

Kurkela

2008

CDM

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“…Electron beam irradiation is widely used for killing microorganisms, bacteria, and viruses ( Berovic et al, 2002 ; Benson, 2002 ; Feng et al, 2020 ), because its penetration depth and dose can be controlled to comply with environmental protection requirements. Moreover, under controlled irradiation, the virus can be partially or totally inactivated, providing useful information on its properties ( Lidzey et al, 1995 ; Smolko and Lombardo, 2005 ).…”

Section: Introductionmentioning

confidence: 99%

Calculations of energy deposition and ionization in the 2019 novel coronavirus by electron beam irradiation

Zhang

Fang

Weng

et al. 2020

Radiation Physics and Chemistry

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Using Monte Carlo methods, this study investigates energy deposition of energetic electrons and ionization in the 2019 novel coronavirus by electron irradiation, which are important characteristic quantities related with biological damage formation. The inelastic scattering of low-energy electrons (<10 keV) was calculated by dielectric theory. The optical energy-loss functions of viral proteins and RNA were derived from an empirical method in the energy-loss range <40 eV and the calculation of optical parameters of the biomolecules. The densities and distributions of energy deposition and ionization were calculated from the stopping power and inelastic cross-sections in the electron-cascade simulation. Electrons with primary energies of approximately 1–3 keV produced significant energy deposition and ionization in the target coronavirus. More energetic electrons were less effective due to the larger electron range and fewer scattering events in the coronavirus.

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“…It was specifically stated that mass was the appropriate parameter (Steer et al, 1980;Beauregard et al, 1987), and a theoretical physics explanation for this was put forth (Kempner and Haigler, 1985). Nevertheless, the "volume" concept has persisted (Bradbury and Zammit, 1990;Lidzey et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

“…This implied that the volume of the unit per se was not involved. The original volume concept has not been abandoned and some radiation studies still refer to the radiation-sensitive volume (Bradbury and Zammit, 1990;Lidzey et al, 1995). There are proteins that significantly change their hydrodynamic properties at different pH.…”

Section: Introductionmentioning

confidence: 99%

Molecular Mass and Volume in Radiation Target Theory

Osborne

Miller

Kempner

2000

Biophysical Journal

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Radiation target analysis is based on the action of ionizing radiation directly on macromolecules. Interactions of this radiation with the molecules leads to considerable structural damage and consequent loss of biological activity. The radiation sensitivity is dependent on the size of the macromolecules. There has been confusion and discrepancy as to whether the molecular mass or the molecular volume was the determinant factor in the sensitivity. Some proteins are known to change their hydrodynamic volume at low pH, and this characteristic can be utilized to compare the radiation sensitivities of these proteins in the two states. The results show that the radiation sensitivity of proteins depends on the mass of the molecule and is independent of the molecular volume/shape.

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A Critical Analysis of the Use of Radiation Inactivation to Measure the Mass of Protein

Cited by 11 publications

References 7 publications

The UDP-Glucuronosyltransferases as Oligomeric Enzymes

The UDP-Glucuronosyltransferases as Oligomeric Enzymes

Calculations of energy deposition and ionization in the 2019 novel coronavirus by electron beam irradiation

Molecular Mass and Volume in Radiation Target Theory

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