Acid phosphatase from maize scutellum: Properties as a function of seed germination |
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| Affiliation: | 1. Department of Pathology, Massachusetts General Hospital, Boston, MA 02114;2. Department of Obstetrics and Gynecology, Division of Maternal Fetal Medicine, Massachusetts General Hospital, Boston, MA 02114;3. Tufts University, Medford, MA 02155;1. Donders Centre of Cognition, Radboud University Nijmegen, Nijmegen, The Netherlands;2. Department of Pharmacology, School of Medicine, Marmara University, Istanbul, Turkey;3. Department of Neurology, Vanderbilt University, Nashville, TN, USA |
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| Abstract: | Acid phosphatase (optimum pH at 5.2) purified from maize scutellum both in a state of dormancy and during the first 24 hours of seed germination has a M, of ca 65000, contains 6% neutral sugar, maintains its catalytic activity after succinylation of 52 free amino groups per molecule and does not show the apparent movement of optimum pH from 5.4 to 6.7 in the presence of 4 mM fluoride. Kinetic data showed Michaelian behaviour for the enzymatic hydrolysis of PNP-P and an apparent number of Pi bound per molecule equal to one. Our results also suggest that the increased acid phosphatase activity in maize scutellum as a function of seed germination could be the result of modifications in the enzyme molecule. |
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