Ca2+ and Mn2+ mediated binding of the glycoprotein peroxidase to membranes of Pharbitis cotyledons |
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Authors: | S. Kiefer C. Penel H. Greppin |
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Affiliation: | Laboratoire de Physiologie végétale, Université de Genève, 3, Place de l''Université, 1211 Geneve, Switzerland |
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Abstract: | Ca2+ and Mn2+ promote the binding of the basic isoperoxidase to a crude membrane preparation in extracts from Pharbitis cotyledons. The Ca2+- or Mn2+-induced binding is resistant to high ionic strength and can be saturated by increasing the divalent ion or the isoperoxidase concentrations. Treatments in vitro with glucosaminidase or in vivo with tunicamycin show that the carbohydrate part of the isoperoxidase is necessary for the binding. The amino sugar galactosamine inhibits the binding at rather high concentrations. Pharbitis basic isoperoxidase can be bound to zucchini squash microsomes in the presence of Ca2+ and conversely. |
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Keywords: | membrane-bound isoperoxidase glycoprotein EGTA MOPS morpholinopropane sulfonic acid |
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