Allophycocyanin B (λmax 671, 618 nm) - A new cyanobacterial phycobiliprotein

A. N. Glazer, D. A. Bryant

Research output: Contribution to journalArticle

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Abstract

A hitherto undescribed red fluorescent phycobiliprotein (maximum emission at ∼ 680 nm), characterized by long wavelength absorption maxima in the visible region at 671 nm (ε=172000 M-1·cm-1 per monomer of mol. wt. 30600) and 618 nm, has been purified to homogeneity from a unicellular cyanobacterium, Synechococcus sp., and from a filamentous cyanobacterium, Anabaena variabilis. The name allophycocyanin B has been proposed for the new protein. A. variabilis allophycocyanin B is characterized by a native molecular weight of 89000 ± 5000 (in 0.05 M phosphate at pH 7.2), an isoelectric point of 5.09, and a subunit molecular weight, based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, of 15300. The protein contains one phycocyanobilin chromophore per subunit. In common with allophycocyanin from the same organism, allophycocyanin B does not contain either histidine or tryptophan. In other respects, the amino acid compositions of the two proteins are significantly different. Synechococcus sp. (Anacystis nidulans) allophycocyanin B gives two components of 16000 and 17000 mol. wt., of equal staining intensity, on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Allophycocyanins B from both organisms cross-react with rabbit antisera directed against either Synechococcus sp. or Anabaena sp. allophycocyanin, but not with antisera against the phycocyanins of the same organisms. It is suggested that allophycocyanin B occupies a position between allophycocyanin and chlorophyll a in the energy transfer path from the accessory pigments to species of chlorophyll a with absorption maxima at λ>670 nm.

Original languageEnglish (US)
Pages (from-to)15-22
Number of pages8
JournalArchives of Microbiology
Volume104
Issue number1
DOIs
StatePublished - Jan 1 1975

Fingerprint

Phycobiliproteins
Synechococcus
Anabaena variabilis
Cyanobacteria
Electrophoresis
Sodium Dodecyl Sulfate
Immune Sera
Polyacrylamide Gel Electrophoresis
Molecular Weight
Molecular weight
Anabaena
Proteins
Energy Transfer
Isoelectric Point
Accessories
Chromophores
Histidine
Pigments
Tryptophan
Energy transfer

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

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title = "Allophycocyanin B (λmax 671, 618 nm) - A new cyanobacterial phycobiliprotein",
abstract = "A hitherto undescribed red fluorescent phycobiliprotein (maximum emission at ∼ 680 nm), characterized by long wavelength absorption maxima in the visible region at 671 nm (ε=172000 M-1·cm-1 per monomer of mol. wt. 30600) and 618 nm, has been purified to homogeneity from a unicellular cyanobacterium, Synechococcus sp., and from a filamentous cyanobacterium, Anabaena variabilis. The name allophycocyanin B has been proposed for the new protein. A. variabilis allophycocyanin B is characterized by a native molecular weight of 89000 ± 5000 (in 0.05 M phosphate at pH 7.2), an isoelectric point of 5.09, and a subunit molecular weight, based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, of 15300. The protein contains one phycocyanobilin chromophore per subunit. In common with allophycocyanin from the same organism, allophycocyanin B does not contain either histidine or tryptophan. In other respects, the amino acid compositions of the two proteins are significantly different. Synechococcus sp. (Anacystis nidulans) allophycocyanin B gives two components of 16000 and 17000 mol. wt., of equal staining intensity, on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Allophycocyanins B from both organisms cross-react with rabbit antisera directed against either Synechococcus sp. or Anabaena sp. allophycocyanin, but not with antisera against the phycocyanins of the same organisms. It is suggested that allophycocyanin B occupies a position between allophycocyanin and chlorophyll a in the energy transfer path from the accessory pigments to species of chlorophyll a with absorption maxima at λ>670 nm.",
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Allophycocyanin B (λmax 671, 618 nm) - A new cyanobacterial phycobiliprotein. / Glazer, A. N.; Bryant, D. A.

In: Archives of Microbiology, Vol. 104, No. 1, 01.01.1975, p. 15-22.

Research output: Contribution to journalArticle

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N2 - A hitherto undescribed red fluorescent phycobiliprotein (maximum emission at ∼ 680 nm), characterized by long wavelength absorption maxima in the visible region at 671 nm (ε=172000 M-1·cm-1 per monomer of mol. wt. 30600) and 618 nm, has been purified to homogeneity from a unicellular cyanobacterium, Synechococcus sp., and from a filamentous cyanobacterium, Anabaena variabilis. The name allophycocyanin B has been proposed for the new protein. A. variabilis allophycocyanin B is characterized by a native molecular weight of 89000 ± 5000 (in 0.05 M phosphate at pH 7.2), an isoelectric point of 5.09, and a subunit molecular weight, based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, of 15300. The protein contains one phycocyanobilin chromophore per subunit. In common with allophycocyanin from the same organism, allophycocyanin B does not contain either histidine or tryptophan. In other respects, the amino acid compositions of the two proteins are significantly different. Synechococcus sp. (Anacystis nidulans) allophycocyanin B gives two components of 16000 and 17000 mol. wt., of equal staining intensity, on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Allophycocyanins B from both organisms cross-react with rabbit antisera directed against either Synechococcus sp. or Anabaena sp. allophycocyanin, but not with antisera against the phycocyanins of the same organisms. It is suggested that allophycocyanin B occupies a position between allophycocyanin and chlorophyll a in the energy transfer path from the accessory pigments to species of chlorophyll a with absorption maxima at λ>670 nm.

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