© 1991 Heron Publishing—Victoria, Canada
Storage protein changes during zygotic embryogenesis in interior spruce
Barry S. Flinn (1, 2), Dane R. Roberts (1), David T. Webb (1, 3) and Ben C. S. Sutton (1)
1. Forest Biotechnology Centre, British Columbia Research Corporation, 3650 Wesbrook Mall, Vancouver, B.C., Canada V6S 2L2 / 2. Author to whom correspondence should be addressed / 3. Forest Biology Division, The Institute of Paper Science and Technology, 575 14th Street NW, Atlanta, GA 30318, USA / Received June 12, 1989
Summary
The major storage proteins isolated from protein bodies of embryo tissues of interior spruce Picea glauca (Moench) Voss/Picea engelmanii Parry had apparent molecular weights of 41, 35, 33, 24 and 22 kD. Minor proteins of 30 and 27.5 kD were also observed. Based
on their solubility characteristics, the 41 kD protein was identified as a water and buffer-soluble albumin, and the 35, 33,
24 and 22 kD proteins were characterized as buffer-insoluble, high salt-soluble globulins. Two-dimensional electrophoresis
revealed each protein was composed of several isoelectric variants. Developmentally specific accumulation of storage proteins
was observed during embryogenesis. The 41 kD protein only accumulated during the later stages of cotyledon maturation, whereas
the other storage proteins began to accumulate during the early stages of embryo development. All storage proteins showed
major accumulations during cotyledon maturation.
