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ALLOPHYCOCYANIN FORMS ISOLATED FROM NOSTOC SP. PHYCOBILISOMES *
Author(s) -
Zilinskas B. A.,
Zimmerman B. K.,
Gantt E.
Publication year - 1978
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1978.tb07650.x
Subject(s) - allophycocyanin , phycobilisome , absorbance , chemistry , nostoc , fluorescence , phycobiliprotein , chromatography , microbiology and biotechnology , phycocyanin , cyanobacteria , biology , genetics , physics , quantum mechanics , bacteria
— Allophycocyanin from dissociated phycobilisomes of Nostoc sp. occurs in three spectrally identifiable forms that fractionate on calcium phosphate adsorption chromatography as: allophycocyanin (APC) I (15–20%), APC II (4&50%), and APC III (30–40%). APC I has a single absorption maximum at 654 nm, and a fluorescence emission peak at 678 nm. The absorption peaks of APC II and III are both at 650 nm, but the relative absorbance at 620/650 nm of APC III is less than that of APC II. The emission of both is maximum at 660 nm. On zone sedimentation in sucrose, their S 20,w values of 6.0 ± 0.1 (APC I), 5.0 ± 0.1 (APC II), and 5.3 ± 0.2 (APC III) were comparable to the order of their elution from Sephadex G‐200. On SDS acrylamide gel electrophoresis two subunits were resolved with apparent molecular weights of 16,900 and 18,400 daltons. When stained by Coomassie blue, they were present in a ratio of 1α:1β in APC II and III, and a probable ratio of 2a:3β in APC I. The larger size of APC I may be accounted for by additional β subunits, by the presence of an additional polypeptide of 35,000 daltons, or both. Over several days, bleaching as noted by a decrease in absorbance at 650 nm, occurred in all three forms; in addition, the more pronounced bleaching at 650 nm, relative to 620 nm, results in APC III becoming spectrally identical to APC II. A trace of a fourth pigment, probably comparable to allophycocyanin‐B, was occasionally detected. The results suggest that several in vitro APC forms (sharing similar subunits) arise upon phycobilisome dissociation, and that APC I is the form most closely related to the final fluorescence emitter of intact phycobilisomes. In this form it probably serves as the bridging pigment in energy transfer from the phycobilisomes to chlorophyll.

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