The light-harvesting antenna of brown algae: highly homologous proteins encoded by a multigene family.

Accessory light-harvesting complexes (LHCFs) were isolated from the brown alga Laminaria saccharina. Complexes specifically associated with photosystem I or II are identical with each other with respect to molecular mass, isoelectric point and behavior on anion-exchange chromatography or non-denaturing isoelectric focusing. The purified complexes also have similar pigment composition and spectroscopic properties.

Gene structure of a chlorophyll a/c-binding protein from a brown alga: presence of an intron and phylogenetic implications.

A Laminaria saccharina genomic library in the phage EMBL 4 was used to isolate and sequence a full-length gene encoding a fucoxanthin-chlorophyll a/c-binding protein. Contrary to diatom homologues, the coding sequence is interrupted by an intron of about 900 bp which is located in the middle of the transit peptide. The deduced amino acid sequence of the mature protein is very similar to those of related proteins from Macrocystis pyrifera (Laminariales) and, to a lesser extent, to those from diatoms and Chrysophyceae.

Fucoxanthin-chlorophyll a/c light-harvesting complexes of Laminaria saccharina: partial amino acid sequences and arrangement in thylakoid membranes.

The N-terminus of the major polypeptide component of the light-harvesting complex (LHC) from the brown alga Laminaria saccharina is blocked. Two partial sequences, one near the N-terminus and the other near the C-terminus, have been obtained by chemical cleavage with acetic acid and N-chlorosuccinimide. Four peptides were separated after trypsin digestion of the thylakoid membranes.

Isolation and characterization of PSII core complexes from a brown alga, Laminaria saccharina.

PSII-enriched particles, active for DCIP-reduction, were prepared from Laminaria saccharina chloroplasts, and PSII core complexes were further purified by ion-exchange chromatography. They contained several polypeptides, four of them cross-reacting with antibodies raised against CP47, CP43, D1 and D2 of green plants. A second chromatography was required to separate: (i) a core antenna, composed of 51 kDa polypeptide subunits, binding 11 beta-carotene, 4 chlorophyll (Chl) c and 7 fucoxanthin for 100 Chl a, and reacting with CP47 antibodies; and (ii) a reaction center complex consisting of two main polypeptides of 34 and 36 kDa.

In vitro synthesis of a plant phospholipid transfer protein: a study by high performance liquid chromatography.

In order to study the biosynthesis of a plant phospholipid transfer protein (PLTP), poly (A)+RNAs have been prepared from maize seedlings and translated in vitro with a rabbit reticulocyte lysate. The newly synthesized proteins were then separated by fast protein liquid chromatography (FPLC) followed by SDS-PAGE or by high performance liquid chromatography (HPLC) coupled to a radioactivity detector monitor. It has been showed that a radioactive band comigrating with a 14C methylated pure PLTP was detected by SDS-PAGE.