Legumin- and vicilin-like proteins from spores of the fern Matteuccia struthiopteris.
Legumin- and vicilin-like proteins have been isolated from spores of the fern Matteuccia struthiopteris. Their relationship with seed legumin and vicilin was demonstrated by cross-reactivities of antibodies directed against respective storage globulins from Vicia faba as evidenced by Western blotting. The Matteuccia legumin-like protein was characterised as a 300-340 kDa holoprotein preferentially consisting of a 32 kDa alpha-chain and a 24 kDa beta-chain. Patterns of limited proteolysis of the spore legumin-like protein and seed legumins were similar as well. In contrast to seed legumins, the Matteuccia legumin-like protein is devoid of disulfide bridges between alpha- and beta-chains. A 52 kDa polypeptide of the Matteuccia vicilin-like protein, first detected by SDS gel electrophoresis, is probably encoded by a vicilin-like gene specifically expressed in Matteuccia struthiopteris spores (Shutov et al. 1998). The vicilin-like holoprotein was found to form a complex of 600 kDa apparent molecular mass, presumably composed of four vicilin-like trimers.
Kakhovskaja
Irina
I
State University of Moldova, Mateevich-Str. 60, MD-2009 Kishinev, Moldova.
Rudacova
Angela
A
Manteuffel
Renate
R
D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D029624:Ferns / Q000737:chemistry / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D055314:Seed Storage Proteins; D012639:Seeds / Q000737:chemistry / Q000378:metabolism; D013170:Spores / Q000737:chemistry / Q000378:metabolism*; D031307:Vicia faba / Q000737:chemistry / Q000378:metabolism; D000097793:Legumins
D010940:Plant Proteins; D055314:Seed Storage Proteins; D000097793:Legumins; C015575:vicilin protein, plant