Physico-chemical and immunological properties of allophycocyanins

Cohen-Bazire, Germaine; Beguin, Simone; Rimon, Sara; An, Glazer; Dm, Brown

doi:10.1007/bf00549359

Cited by 89 publications

(33 citation statements)

References 26 publications

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“…Polyacrylamide gel electrophoresis in the presence of urea and densitometry revealed the presence of two subunits in equimolar amounts carrying equal amounts of phycocyanobilin chromophores. A single species with a sedimentation coefficient of 5.2 S (50 mM sodium acetate buffer, pH 5.5) was detected in the analytical ultracentrifuge; thus, the purified allophycocyanin existed in solution as the trimer (@)3 [30,36,40]. Under conditions similar to those described for the crystallization of Anahaena 641 1 allophycocyanin [36], the Pseudanabaena 7409 allophycocyanin also crystallized as needles.…”

Section: Components Of Phycobilisomes Isolated From Cells Grown In Rmentioning

confidence: 97%

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Effects of Chromatic Illumination on Cyanobacterial Phycobilisomes

Bryant

Cohen-Bazire

1981

European Journal of Biochemistry

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Pseudunuhaena 7409 is a chromatically adapting cyanobacterium which photocontrols the synthesis of both phycoerythrin and phycocyanin [Tandeau de Marsac (1 977) J. Bacteriol. 130, 82 -911. Phycobilisomes, isolated from cells grown in either green or red light, have been dissociated and the component biliproteins purified and characterized.Phycobilisomes isolated from cells grown in green light were composed of allophycocyanin B, allophycocyanin, two phycocyanin subunits (one a-type and one j-type subunit), phycoerythrin and eight uncolored polypeptides. When dissociated phycobilisomes were chromatographed on DEAE-cellulose at pH 5.5, most of the phycocyanin was recovered as part of a large (17.3 S) multiprotein complex with phycoerythrin (molar ratio 1 : 1). This complex also contained five of the uncolored polypeptides found in intact phycobilisomes isolated from cells grown in green light.Phycobilisomes isolated from cells grown in red light were composed of allophycocyanin B, allophycocyanin, four phycocyanin subunits (two cc-type and two 0-type subunits), and six uncolored polypeptides. When these phycobilisomes were dissociated, the phycocyanin was recovered as a large (21 .O S) multiprotein complex which was composed of the four phycocyanin subunits types and four uncolored polypeptides. This complex was morphologically identical to the rod-like stacks of discs about 6 x 12 nm which form the peripheral rods of intact phycobilisomes.Each of the four phycocyanin subunits found in the complex isolated from the phycobilisomes of cells grown in red light was purified to homogeneity and characterized. Amino acid compositions of the four subunits indicated that each subunit was a unique gene product. Two of the subunits of the complex were apparently identical to those of the phycocyanin purified from phycobilisomes isolated from cells grown in green light. These studies suggest that one pair of phycocyanin subunits was synthesized constitutively (i.e. irrespective of the light wavelength to which the cells were exposed during growth) while the synthesis of the second pair of phycocyanin subunits was specifically induced during growth in red light.

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Section: Components Of Phycobilisomes Isolated From Cells Grown In Rmentioning

confidence: 97%

“…Electrophoresis at pH 7.85 on 5 "/, polyacrylamide gels in the presence of 8.0 M urea was performed as described by Cohen-Bazire et al [30]. Samples were prepared for electrophoresis as described [8].…”

Section: Polyacrylamide Gel Electrophoresismentioning

confidence: 99%

Effects of Chromatic Illumination on Cyanobacterial Phycobilisomes

Bryant

Cohen-Bazire

1981

European Journal of Biochemistry

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“…Electrophoresis at pH 7.5 on 5 % (w/v) polyacrylamide gels (0.6 x 10 to 12 cm) was performed as described by Cohen-Bazire et al (1977). Isoelectric focusing was performed on photopolymerized 7.0% (w/v) polyacrylamide gels in the pH range 4.0 to 6.0, according to the procedure of Bio-Rad Laboratories (Technical Bulletin 1030, April, 1975.…”

Section: ) Tandeau De Marsacmentioning

confidence: 99%

Phycoerythrocyanin and Phycoerythrin: Properties and Occurrence in Cyanobacteria

1982

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A number of cyanobacterial phycoerythrocyanins were isolated and characterized with respect to spectroscopic properties and chromophore content. All were similar to the phycoerythrocyanin of Anabaena PCC 64 1 1 and cross-reacted strongly with an antiserum prepared against that protein. The synthesis of phycoerythrocyanin was not controlled by a complementary chromatic adaptation mechanism in nine strains tested, but its synthesis appeared to be affected by light intensity. A survey of 240 strains of cyanobacteria revealed that no strain synthesized both phycoerythrocyanin and phycoerythrin and that phycoerythrocyanin was largely confined to those strains which can form heterocysts. Phycoerythrocyanin may be a taxonomically useful marker for certain strain clusters of this cyanobacterial grouping. Spectroscopic properties and chromophore compositions of several cyanobacterial phycoerythrins were also determined. At present, the ability to synthesize phycoerythrin and the capacity to exhibit complementary chromatic adaptation responses are widely distributed traits of limited taxonomic usefulness.

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“…Through the use of monospecific antibodies obtained for each ofthe major spectroscopically distinct biliprotein classes, namely, APC, PC, and PE, a striking conservation of antigenic determinants has been described for those proteins of a given spectroscopic class, irrespective ofalgal source (1,2,4,6). For (14).…”

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confidence: 99%

The Immunologically Conserved Phycobilisome-Thylakoid Linker Polypeptide

Zilinskas

Howell²

1986

Plant Physiol.

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We have isolated phycobilisomes from two classes of red algae, several subdivisions of the cyanobacteria, and the cyanelles of Cyanophora paradoxa. In addition to the major light harvesting biliproteins, these phycobilisomes also contain several other polypeptides, the largest of which ranges from 75 to 120 kilodaltons in the different species surveyed. This protein, previously isolated and characterized from three species, was shown to be the final emitter of excitation energy in phycobilisomes and is also thought to be involved in the attachment of the phycobilisomes to the thylakoid membrane. We have obtained polyclonal antibodies to the 95 kilodalton polypeptide isolated from phycobilisomes of the cyanobacterium, Nostoc sp. This protein shares no common antigenic determinants with either the a or subunits of allophycocyanin, or any of the other biliproteins, as determined by the sensitive Western immunoblotting technique. However, this antiserum cross-reacts with the highest molecular weight polypeptide of all the rhodophytan and cyanobacterial phycobilisomes tested. That these proteins are immunologically related, but are unrelated to other biliproteins, is reminiscent of previous immunological studies of biliproteins which showed that while the three major spectroscopically distinct classes of biliproteins (phycoerythrin, phycocyanin, and allophycocyanin) shared no common antigenic determinants, there was a strong antigenic determinant to specific biliprotein classes which crossed taxonomic divisions.The key pigment of PBsomes2 is APC; its position is analogous to that of the trap ofthe two photosystems, but rather than doing photochemistry, it collects excitation energy from the other biliproteins before funneling it into the Chl ofthe thylakoid. We have previously described a special form of APC, called APC I, which we proposed was the final collector of excitation energy in the PBsome (16 (Fig. la) shows the isolated 95 kD polypeptide (and its 80 kD proteolytic degradation product) in

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Physico-chemical and immunological properties of allophycocyanins

Cited by 89 publications

References 26 publications

Effects of Chromatic Illumination on Cyanobacterial Phycobilisomes

Effects of Chromatic Illumination on Cyanobacterial Phycobilisomes

Phycoerythrocyanin and Phycoerythrin: Properties and Occurrence in Cyanobacteria

The Immunologically Conserved Phycobilisome-Thylakoid Linker Polypeptide

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