Isolation and characterization of biliprotein aggregates from Acaryochloris marina, a Prochloron-like prokaryote containing mainly chlorophyll d

FEBS Lett. 1997 Jun 30;410(2-3):428-32. doi: 10.1016/s0014-5793(97)00631-5.

Abstract

Phycobiliprotein aggregates were isolated from the prokaryote Acaryochloris marina, containing chlorophyll d as major pigment. In the electron microscope the biliprotein aggregates appear as rod-shaped structures of 26.0 x 11.3 nm, composed of four ring-shaped subunits 5.8 nm thick and 11.7 nm in diameter. Spectral data indicate that the aggregates contain two types of biliproteins: phycocyanin and an allophycocyanin-type pigment, with very efficient energy transfer from the phycocyanin- to allophycocyanin-type constituent. The chromophore-binding polypeptides of the pigments have apparent molecular masses of 16.2 and 17.4 kDa. They crossreact with antibodies against phycocyanin and allophycocyanin from a red alga.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / ultrastructure
  • Chlorophyll
  • Cyanobacteria / chemistry*
  • Light-Harvesting Protein Complexes
  • Membrane Proteins / chemistry
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / ultrastructure
  • Phycocyanin / chemistry
  • Plant Proteins / chemistry*
  • Plant Proteins / isolation & purification
  • Plant Proteins / ultrastructure
  • Spectrometry, Fluorescence

Substances

  • Bacterial Proteins
  • Light-Harvesting Protein Complexes
  • Membrane Proteins
  • Plant Proteins
  • allophycocyanin
  • Phycocyanin
  • Chlorophyll
  • chlorophyll d