Calreticulin, the main Ca2+ binding protein in the endoplasmic reticulum of eukaryotic cells, was characterized in Ginkgo biloba L. pollen and seeds. Electrophoretic analysis of the partly purified extracts showed the presence of two protein bands of 57 and 50 kDa apparent molecular masses, which strongly cross-reacted with antibodies against plant calreticulins. Amino acid sequence comparison with other plant and animal calreticulins revealed a much higher similarity of the N-terminus of Ginkgo calreticulins with the homologue from angiosperms rather than with that from mammals. The finding of calreticulin in Ginkgo is indicative of the conservation also in gymnosperms of Ca2+ homeostatic mechanisms, which seem to rely on the same molecular components as all eukaryotic cells.

Ginkgo biloba expresses calreticulin, the major calcium-binding reticuloplasmin in eukaryotic cells.

BALDAN, BARBARA;NAVAZIO, LORELLA;MARIANI, PAOLINA
1998

Abstract

Calreticulin, the main Ca2+ binding protein in the endoplasmic reticulum of eukaryotic cells, was characterized in Ginkgo biloba L. pollen and seeds. Electrophoretic analysis of the partly purified extracts showed the presence of two protein bands of 57 and 50 kDa apparent molecular masses, which strongly cross-reacted with antibodies against plant calreticulins. Amino acid sequence comparison with other plant and animal calreticulins revealed a much higher similarity of the N-terminus of Ginkgo calreticulins with the homologue from angiosperms rather than with that from mammals. The finding of calreticulin in Ginkgo is indicative of the conservation also in gymnosperms of Ca2+ homeostatic mechanisms, which seem to rely on the same molecular components as all eukaryotic cells.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11577/2468539
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