Salt soluble storage proteins were extracted from seeds of Ephedra distachya, Ephedra foeminea, Gnetum gnemon, Gnetum montanum and Welwitschia mirabilis and separated by chromatographic procedures. The molecular weight of the main storage globulin ranges from 300 to 350 kD. Danaturation by SDS resolved the holoprotein in monomers of Mr 40 to 60 kD. Oligomers up to 120 kD were observed in Ephedra. Reduction of disulphide bridges by DTE resolved the monomers in paris of polypeptides of Mr 10 to 35 kD. The characters above indicate that the main storage globulin of Gnetopsida is a legumin-like protein.
Storage globulins in Gnetopsida. 1. Recognition of legumin-iike proteins / Conte L.. - In: GIORNALE BOTANICO ITALIANO. - ISSN 0017-0070. - STAMPA. - 128:5(1994), pp. 839-843. [10.1080/11263509409430307]
Storage globulins in Gnetopsida. 1. Recognition of legumin-iike proteins
Conte L.
1994
Abstract
Salt soluble storage proteins were extracted from seeds of Ephedra distachya, Ephedra foeminea, Gnetum gnemon, Gnetum montanum and Welwitschia mirabilis and separated by chromatographic procedures. The molecular weight of the main storage globulin ranges from 300 to 350 kD. Danaturation by SDS resolved the holoprotein in monomers of Mr 40 to 60 kD. Oligomers up to 120 kD were observed in Ephedra. Reduction of disulphide bridges by DTE resolved the monomers in paris of polypeptides of Mr 10 to 35 kD. The characters above indicate that the main storage globulin of Gnetopsida is a legumin-like protein.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
