التفاصيل البيبلوغرافية
| العنوان: |
Purification of a lipoxygenase from ungerminated barley. Characterization and product formation |
| المؤلفون: |
Vliegenthart, J.F.G., Aarle, P.G.M. van, Barse, M.M.J. de, Veldink, G.A. |
| سنة النشر: |
1991 |
| مصطلحات موضوعية: |
Scheikunde |
| الوصف: |
Lipoxygenase was purified from ungerminated barley (variety ‘Triumph’), yielding an active enzyme with a pl of 5.2 and a molecular mass of approximately 90 kDa. In addition to the 90 kDa band SDS-PAGE showed the presence of two further proteins of 63 kDa. Western blot analysis showed cross-reactivity of each of these proteins with polyclonal antisera against lipoxygenases from pea as well as from soybean, suggesting a close immunological relationship. he 63 kDa proteins appear to be inactive degradation products of the active 90-kDa enzyme. This barley lipoxygenase converts linolcic acid mainly into (9S)-(10E,12Z)-9-hydroperoxy-10, 12-octadecadienoic acid, and arachidonic acid into (5S)-(6E,8Z,11Z,14Z)-5-hydroperoxy-6,8,11,14-cicosatetraenoic acid. |
| نوع الوثيقة: |
article in journal/newspaper |
| وصف الملف: |
text/plain |
| اللغة: |
English |
| تدمد: |
0014-5793 |
| Relation: |
https://dspace.library.uu.nl/handle/1874/5552 |
| الاتاحة: |
https://dspace.library.uu.nl/handle/1874/5552 |
| Rights: |
info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: |
edsbas.48E8C0DC |
| قاعدة البيانات: |
BASE |
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