Comparison of stability properties of lactate dehydrogenase B4/e-crystallin from different species
| العنوان: | Comparison of stability properties of lactate dehydrogenase B4/e-crystallin from different species |
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| المؤلفون: | Christina E.M. Voorter, Liesbeth T. Wintjes, Hans Bloemendal, Wilfried W. de Jong, Pieter W. H. Heinstra |
| المصدر: | European Journal of Biochemistry. 211:643-648 |
| بيانات النشر: | Wiley, 1993. |
| سنة النشر: | 1993 |
| مصطلحات موضوعية: | Hot Temperature, animal structures, Swine, Molecular Sequence Data, Biology, Biochemistry, Isozyme, Lens protein, chemistry.chemical_compound, Crystallin, Lactate dehydrogenase, Enzyme Stability, Lens, Crystalline, Animals, Amino Acid Sequence, Thermostability, chemistry.chemical_classification, L-Lactate Dehydrogenase, Myocardium, Crystallins, Enzyme assay, Isoenzymes, Kinetics, Ducks, Enzyme, chemistry, Urea, biology.protein, Chickens |
| الوصف: | epsilon-Crystallin occurs as an abundant lens protein in many birds and in crocodiles and has been identified as heart-type lactate dehydrogenase (LDH-B4). Lens proteins have, due to their longevity and environmental conditions, extraordinary requirements for structural stability. To study lens-protein stability, we compared various parameters of LDH-B4/epsilon-crystallin from lens and/or heart of duck, which has abundant amounts of this enzyme in its lenses, and of chicken and pig, which have no epsilon-crystallin. Measuring the thermostability of LDH-B4 from the different sources, the t50 values (temperature at which 50% of the enzyme activity remains after a 20-min period) for LDH-B4 from duck heart, duck lens and chicken heart were all found to be around 76 degrees C, whereas pig heart LDH-B4 was less thermostable, having a t50 value of 62.5 degrees C. A similar tendency was found with urea inactivation studies. Plotting the first-order rate constants obtained from inactivation kinetic plots against urea concentration, it was clear that LDH-B4 from pig heart was less stable in urea than the homologous enzymes from duck heart, chicken heart and duck lens. The duck and chicken enzymes were also much more resistant against proteolysis than the porcine enzyme. Therefore, it is concluded that avian LDH-B4 is structurally more stable than the homologous enzyme in mammals. This greater stability might make it suitable to function as a crystallin, as in duck, but is not necessarily associated with high lens expression, as in chicken. |
| تدمد: | 1432-1033 0014-2956 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92b999f2fb29a57d6a52f3f98f5a79a3Test https://doi.org/10.1111/j.1432-1033.1993.tb17592.xTest |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....92b999f2fb29a57d6a52f3f98f5a79a3 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14321033 00142956 |
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