Three glycosylated polypeptides secreted by several embryogenetic cell cultures of pine show highly specific serological affinity to antibodies directed against the wheat germin apoprotein monomer

• Published in: Plant physiology (Bethesda) Vol. 108; no. 1
• Main Authors: Domon, J.M. (Universite de Picardie Jules Verne, Amiens, France.), Dumas, B, Laine, E, Meyer, Y, David, A, David, H
• Format: Journal Article
• Language: English
• Published: 01.05.1995
• Subjects: ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; ANTICORPS; ANTICUERPOS; COMPOSICION QUIMICA; COMPOSITION CHIMIQUE; CULTIVO DE CELULAS; CULTURE DE CELLULE; EMBRIONES VEGETALES; EMBRYON VEGETAL; IMMUNOLOGIE; INMUNOLOGIA; LIPOPROTEINAS; LIPOPROTEINE; OXALATE; OXALATOS; OXIDORREDUCTASAS; OXYDOREDUCTASE; PEPTIDE; PEPTIDOS; PINUS CARIBAEA; PROTEINAS; PROTEINE; SECRECIONES DE LAS PLANTAS; SECRETION VEGETALE; VARIACION GENETICA; VARIATION GENETIQUE
• ISSN: 0032-0889

Embryogenic tissues of Pinus caribaea Morelet var hondurensis produce extracellular proteins; among them germins have been identified. Two-dimensional electrophoresis followed by electroblotting onto a polyvinylidene difluoride membrane allowed isolation and N-terminal amino acid sequencing of extracellular GP111, which is present within the five embryogenic cell lines studied. The amino acid sequence showed strong homologies with the sequences of germins deduced from cDNA sequencing, starting at the same amino acid position but one, compared with other sequences of mature germins deduced from protein sequencing. Immunoblots of embryogenic and nonembryogenic extracellular proteins indicated that the polypeptide GP111 plus two others with similar relative molecular mass values are present in embryogenic cell lines but not in nonembryogenic ones. They were recognized by an antiserum raised against the nonglycosylated monomer of wheat germin. The cross-reaction between pine and wheat apoproteins was highly specific. An antiserum against the glycosylated pentameric germin-like protein (an oxalate oxidase) of barley cross-reacted with all three, as well as with several other glycosylated polypeptides