Recovery of soluble proteins from glanded cotton tissues with amines |
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| Authors: | J H Schmidt R Wells |
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| Affiliation: | 1. Department of Environmental Health Sciences, Yale School of Public Health, 60 College Street, New Haven, CT, 06520-8034, USA;2. Yale Center on Climate Change and Health, Yale School of Public Health, 60 College Street, New Haven, CT, 06520-8034, USA;3. China CDC Key Laboratory of Environment and Population Health, National Institute of Environmental Health, Chinese Center for Disease Control and Prevention, Beijing, 100021, China;4. Beijing Municipal Health Commission Information Center, Beijing, 100034, China;1. Virginia Center for Coal and Energy Research, Blacksburg, VA, USA;2. Virginia Tech Department of Mining and Minerals Engineering, Blacksburg, VA, USA;3. Marshall Miller and Associates Inc., Bluefield, VA, USA;1. College of Chemistry and Materials Science, Hengyang Normal University, Hengyang 421001, China;2. Hunan Engineering Research Center for Monitoring and Treatment of Heavy Metals Pollution in the Upper Reaches of Xiangjiang River, Hengyang 421001, China;3. State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China;4. Institute of Analytical Food Safety, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China;5. Key Laboratory of Synthetic and Biological Colloids, Ministry of Education, School of Chemical and Material Engineering, Jiangnan University, Wuxi 214122, China;1. Department of Chemistry, Faculty of Engineering, Istanbul University-Cerrahpasa, Avcilar 34320, Istanbul, Turkey;2. Turkish Academy of Sciences (TUBA), Vedat Dalokay Cad. No. 112, Cankaya, 06670 Ankara, Turkey |
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| Abstract: | A simple soluble protein extraction method was developed for glanded cotton (Gossypium hirsutum L.) tissues. Gossypol, a major component of glands, is known to crosslink and precipitate proteins in cotton tissue homogenates. Established phenolic removal reagents were evaluated as gossypol binding agents and found to be less than effective in enhancing cotton leaf-soluble protein recovery. Several other amines, including a number of affinity support bound amines, were tested and found relatively ineffectual when compared with urea as cotton protein protectants. Urea and (NH4)2SO4, the next most active agent found in the study, were compared on both whole-leaf homogenates and artificial mixtures containing known quantities of poly-L-lysine and a clathrate of gossypol and acetic acid. Urea treatment resulted in both an increased number of stained bands and more concentrated staining of bands than any other treatment on polyacrylamide gels. Selected enzymes demonstrated increased activities in urea homogenates compared with other treatments. |
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