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Immunocytochemical Localization of Phycoerythrin‐545 and of a Chlorophyll a/c Light Harvesting Complex in Cryptomonas maculata (Cryptophyceae)
Author(s) -
Rhiel E.,
Kunz J.,
Wehrmeyer W.
Publication year - 1989
Publication title -
botanica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 0932-8629
DOI - 10.1111/j.1438-8677.1989.tb00066.x
Subject(s) - phycoerythrin , thylakoid , biology , chlorophyll a , phycobiliprotein , botany , immunogold labelling , chlorophyll , phycocyanin , biochemistry , cyanobacteria , microbiology and biotechnology , chloroplast , ultrastructure , bacteria , flow cytometry , genetics , gene
Antisera, raised against the subunits of phycoerythrin‐545 and total chlorophyll a/c light harvesting complex (chl a/c LHC) of Cryptomonas maculata , were tested for specificity by immunodiffusion and Western‐immunoblotting experiments. They were further used for immunogold‐labeling of Lowicryl sections of control and nitrogen deficient cells. In control cells (+ N) the antiserum against the chl a/c LHC labeled the thylakoid membranes uniformly. On the other hand, the label against the subunits of the water soluble phycoerythrin‐545 was almost completely restricted to the thylakoid lumen. Nitrogen deficient cells (–N) compared to control cells exhibited labels against the chl a/c LHC with very similar densities per unit area. For the subunits of phycoerythrin‐545 a three‐ to four‐fold weaker gold label per unit area was measured. These results confirm some of the earlier conclusions, e.g. the persistence of the chl a/c LHC even under conditions of nitrogen‐deficiency and the extensive degradation of the biliprotein (Rhiel et al., 1985, 1986, 1987).