Open AccessHigher plant chloroplasts: Evidence that all the chlorophyll exists as chlorophyll—protein complexes
Author(s) -
John Markwell,
J. Philip Thornber,
Russell T. Boggs
Publication year - 1979
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.76.3.1233
Subject(s) - thylakoid , chlorophyll , chloroplast , sodium dodecyl sulfate , chlorophyll a , gel electrophoresis , polyacrylamide gel electrophoresis , light harvesting complexes of green plants , electrophoresis , photosynthesis , chemistry , biochemistry , chlorophyll b , pigment , chromatography , biology , botany , enzyme , organic chemistry , gene
By using the polyacrylamide gel electrophoresis system described in this report, it was possible to fractionate all the photosynthetic pigments of maize (Zea mays L.) thylakoids into chlorophyll—protein complexes with negligible formation of free or detergent-complexed chlorophyll. Identical sodium dodecyl sulfate extracts of thylakoids have previously resulted in up to 50% of the chlorophyll migrating as free chlorophyll after electrophoresis. The major difference from previous gel electrophoresis systems is the replacement of sodium dodecyl sulfate in the electrophoresis buffer by Deriphat 160 (disodiumN -lauryl-β-iminodipropionate), a zwitterionic detergent. The results suggest that: (i ) no significant amount of free chlorophyll exists in the chloroplast thylakoid membranesin vivo , and (ii ) most of the free pigment seen previously on gels was generated during the electrophoresis and was not a result of the solubilization technique. Additionally, the new chlorophyll-protein complexes resolved appear to have different characteristics (pigment content and size) that those observed in former systems.