Quantitative and qualitative aspects of peroxidases extracted from cladodes of Opuntia ficus indica |
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| Institution: | 1. State Key Laboratory of Heavy Oil Processing, College of Science, China University of Petroleum, Beijing 102249, PR China;2. College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, PR China;3. Department of Physics and Center for Marine-Integrated Biomedical Technology, Pukyong National University, Busan 608-737, Republic of Korea;1. Neurology Unit, Bambino Gesù Children''s Hospital, Rome, Italy;2. Pathology Unit, Bambino Gesù Children''s Hospital, Rome, Italy;3. Neurosurgery Unit, Bambino Gesù Children''s Hospital, Rome, Italy;1. Gilbert and Rose-Marie Chagoury School of Medicine, Lebanese American University Medical Center, Beirut, Lebanon;2. Division of Rheumatology, Faculty of Medicine, American University of Beirut, Beirut, Lebanon;1. Bio-wave Research Center, Department of Laboratory Medicine, Third Military Medical University, Chongqing 400038, China;2. Chongqing Family Planning Committee, Chongqing 400036, China;1. Houston Methodist Research Institute, 6670 Bertner Ave, Houston, TX 77030, USA;2. Centers for Disease Control and Prevention, 1600 Clifton Rd, Atlanta, GA 30333, USA;3. Emory University School of Medicine, 1648 Pierce Dr NE, Atlanta, GA 30307, USA;4. Maryland Department of Health and Mental Hygiene, 201 W Preston St, Baltimore, MD 21201, USA |
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| Abstract: | Peroxidases (EC 1.11.1.7) were extracted from fresh cladodes harvested from nine ecotypes of the cactus species Opuntia ficus indica Mill. growing as a collection, in Marrakech (South Morocco). Two enzyme fractions were obtained by a progressive solubility method leading to soluble peroxidases (S) and ionically wall-bound peroxidases (I). The preferred substrate for cladode peroxidases was determined to be o-dianisidine over 4-chloro-1-naphtol and guaiacol. Contrarily to roots, no guaiacol-based activity was found in cladodes. The late ecotypes 1‘Haddaouia’ and ‘Moussa’ showed a relatively high peroxidase ratio S/I (units g−1 fresh weight). When subjected to electrophoresis on polyacrylamide gels, S and I peroxidase fractions each exhibited two enzyme forms based on their electric charges in basic and acidic gel media. Acidic peroxidase forms, well separated on basic gels, showed two principal migration zones with great differences in their enzyme activities depending on the fraction types S and I. Acidic ionically wall-bound peroxidases exhibited fast, highly active isoforms with Rf values 0.42–0.58. Basic forms, represented essentially in fractions S and resolved on acidic gels, were typified by slow and fast isoforms with a double banded pattern in most ecotypes. Opuntia ecotypes collected from localities surrounding Marrakech exhibited fast basic soluble isoforms, while distant ecotypes from Marrakech, including late ones, were typified by a fast acidic ionically bound isoperoxidase of Rf 0.58. Possible roles of O. f. indica peroxidases in growth and their evaluation as markers in this cactus species are discussed in this study. |
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