Calcium ions and polyamines activate the plasma membrane-located 1,3-beta-glucan synthase [Glycine max]

• Published in: Planta 1987-05, Vol.171 (1), p.130-135
• Main Authors: Fink, J. (Kaiserslautern Univ. (Germany, F.R.). Fachbereich Biologie), Jeblick, W, Blaschek, W, Kauss, H
• Format: Article
• Language: English
• Subjects: 1,3- beta -D-glucan synthase; ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; AMINAS; AMINE; AMINES; Analytical, structural and metabolic biochemistry; Biological and medical sciences; CALCIO; CALCIUM; Calciumion; Cell membranes; CELL WALLS; Chemical suspensions; Enzymaktivitaet; Enzymes; Enzymes and enzyme inhibitors; ENZYMIC ACTIVITY; Fundamental and applied biological sciences. Psychology; Glucans; Glycine; GLYCINE MAX; Glycine soja; Kallosesynthese; Microsomes; PARED CELULAR; PAROI CELLULAIRE; Plants; Plasma density; Plasmamembran; Polyamin; Polyamines; Soybeans; Suspensionskultur; Transferases; Zelle
• ISSN: 0032-0935; 1432-2048
• DOI: 10.1007/BF00395076

Sucrose-density-gradient centrifugation and partitioning in a polyethylene glycol/dextran two-phase system were used to isolate plasma-membrane vesicles from microsomal preparations of soybean cell suspension cultures. Both methods resulted in the enrichment of the activity of a 1,3-β-glucan synthase which forms a polymer consisting of more than 99% of 1,3-linked glucose (callose). Digitonin increases the 1,3-β-glucan synthase activity in the various membrane fractions to a different degree, supporting the suggestion that this enzyme is vectorially arranged in the plasma membrane. The enzyme is greatly activated either by poly-L-ornithine or synergistically by Ca2+ and spermine, indicating that the same enzyme is affected and exhibits the regulatory properties necessary for callose synthesis.