title: Immunodetection and photostability of NADPH-protochlorophyllide oxidoreductase in Pinus pinea L.
abstract: Antibody against the light-dependent NADPH-protochlorophyllide oxidoreductase of oat was used to detect a protein of the same molecular weight in cotyledons of 40-day-old dark-grown seedlings of Pinus pinea L. Exposure of the seedlings to light resulted in a rapid decrease in protochlorophyllide content without the concomitant decrease in 38 kDa protein which is observed on transfer of dark-grown angiosperm seedlings to light. The stability of the light-dependent NADPH-protochlorophyllide oxidoreductase in pine in the absence of accumulated substrate is consistent with either (1) a different mechanism of regulation of chlorophyll synthesis in gymnosperms or (2) a higher proportion of stable extra-plastidic protein reacting with the antibody to the light-dependent NADPH-protochlorophyllide oxidoreductase than is the case in angiosperms.
authors.affiliation: School of Biological Science, Macquarie University, 2109, Sydney, N.S.W., Australia.
authors.forename: K
authors.initials: K
authors.lastname: Ou
authors.forename: N
authors.initials: N
authors.lastname: Packer
authors.forename: H
authors.initials: H
authors.lastname: Adamson