Protein composition of intact and fractionated memberanes isolated from dark and light grown cells of a blue green mutant of Rhodospirillum Rubrum (BG1)
1. By means of different fractionation procedures we have separated two major protein fractions present in photosynthetically grown cells of the blue-green mutant of Rhodospirillum rubrum (BG1). These proteins are found in differing amounts in the two subchromatophore fragments produced by the deter...
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todo:paper_00052728_v256_n1_p108_Kerber2023-10-03T14:03:14Z Protein composition of intact and fractionated memberanes isolated from dark and light grown cells of a blue green mutant of Rhodospirillum Rubrum (BG1) Kerber, N.L. García, A.F. Vernon, L.P. Raveed, D. bacterial protein chlorophyll Surface Active Agents surfactant trypsin urea adaptation article bacterial chromatophore cell fractionation cytology darkness electron microscopy gel electrophoresis light membrane metabolism mutation osmosis photosynthesis radiation exposure radiation response Rhodospirillum Rhodospirillum rubrum Adaptation, Physiological Bacterial Chromatophores Bacterial Proteins Cell Fractionation Chlorophyll Darkness Electrophoresis, Disc Light Membranes Microscopy, Electron Mutation Osmosis Photosynthesis Radiation Effects Rhodospirillum Rhodospirillum rubrum Subcellular Fractions Surface-Active Agents Trypsin Urea 1. By means of different fractionation procedures we have separated two major protein fractions present in photosynthetically grown cells of the blue-green mutant of Rhodospirillum rubrum (BG1). These proteins are found in differing amounts in the two subchromatophore fragments produced by the detergent Triton X-100. A more extensive breakdown caused by digestion of intact photosynthetic membrane with Triton X-100 and trypsin produced four main protein fractions which were separated by means of gel electrophoresis. Some of these bands originated from proteins that were intimately associated with bacteriochlorophyll in the intact membrane. The other protein fractions seem to derive from a group of proteins whose function could be a supporting one. These protein fractions seem to be a somewhat degraded form of the basic membrane core that cannot be further attacked by the combined action of the detergent and the trypsin. 2. Electron micrographs of the fractions obtained by the digestion with Triton X-100 and trypsin are presented, showing a very different structure for the degraded basic membrane and a unique structure for the aggregated units of the bacteriochlorophyll-containing fraction. © 1972. Fil:Kerber, N.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:García, A.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00052728_v256_n1_p108_Kerber |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
bacterial protein chlorophyll Surface Active Agents surfactant trypsin urea adaptation article bacterial chromatophore cell fractionation cytology darkness electron microscopy gel electrophoresis light membrane metabolism mutation osmosis photosynthesis radiation exposure radiation response Rhodospirillum Rhodospirillum rubrum Adaptation, Physiological Bacterial Chromatophores Bacterial Proteins Cell Fractionation Chlorophyll Darkness Electrophoresis, Disc Light Membranes Microscopy, Electron Mutation Osmosis Photosynthesis Radiation Effects Rhodospirillum Rhodospirillum rubrum Subcellular Fractions Surface-Active Agents Trypsin Urea |
spellingShingle |
bacterial protein chlorophyll Surface Active Agents surfactant trypsin urea adaptation article bacterial chromatophore cell fractionation cytology darkness electron microscopy gel electrophoresis light membrane metabolism mutation osmosis photosynthesis radiation exposure radiation response Rhodospirillum Rhodospirillum rubrum Adaptation, Physiological Bacterial Chromatophores Bacterial Proteins Cell Fractionation Chlorophyll Darkness Electrophoresis, Disc Light Membranes Microscopy, Electron Mutation Osmosis Photosynthesis Radiation Effects Rhodospirillum Rhodospirillum rubrum Subcellular Fractions Surface-Active Agents Trypsin Urea Kerber, N.L. García, A.F. Vernon, L.P. Raveed, D. Protein composition of intact and fractionated memberanes isolated from dark and light grown cells of a blue green mutant of Rhodospirillum Rubrum (BG1) |
topic_facet |
bacterial protein chlorophyll Surface Active Agents surfactant trypsin urea adaptation article bacterial chromatophore cell fractionation cytology darkness electron microscopy gel electrophoresis light membrane metabolism mutation osmosis photosynthesis radiation exposure radiation response Rhodospirillum Rhodospirillum rubrum Adaptation, Physiological Bacterial Chromatophores Bacterial Proteins Cell Fractionation Chlorophyll Darkness Electrophoresis, Disc Light Membranes Microscopy, Electron Mutation Osmosis Photosynthesis Radiation Effects Rhodospirillum Rhodospirillum rubrum Subcellular Fractions Surface-Active Agents Trypsin Urea |
description |
1. By means of different fractionation procedures we have separated two major protein fractions present in photosynthetically grown cells of the blue-green mutant of Rhodospirillum rubrum (BG1). These proteins are found in differing amounts in the two subchromatophore fragments produced by the detergent Triton X-100. A more extensive breakdown caused by digestion of intact photosynthetic membrane with Triton X-100 and trypsin produced four main protein fractions which were separated by means of gel electrophoresis. Some of these bands originated from proteins that were intimately associated with bacteriochlorophyll in the intact membrane. The other protein fractions seem to derive from a group of proteins whose function could be a supporting one. These protein fractions seem to be a somewhat degraded form of the basic membrane core that cannot be further attacked by the combined action of the detergent and the trypsin. 2. Electron micrographs of the fractions obtained by the digestion with Triton X-100 and trypsin are presented, showing a very different structure for the degraded basic membrane and a unique structure for the aggregated units of the bacteriochlorophyll-containing fraction. © 1972. |
format |
JOUR |
author |
Kerber, N.L. García, A.F. Vernon, L.P. Raveed, D. |
author_facet |
Kerber, N.L. García, A.F. Vernon, L.P. Raveed, D. |
author_sort |
Kerber, N.L. |
title |
Protein composition of intact and fractionated memberanes isolated from dark and light grown cells of a blue green mutant of Rhodospirillum Rubrum (BG1) |
title_short |
Protein composition of intact and fractionated memberanes isolated from dark and light grown cells of a blue green mutant of Rhodospirillum Rubrum (BG1) |
title_full |
Protein composition of intact and fractionated memberanes isolated from dark and light grown cells of a blue green mutant of Rhodospirillum Rubrum (BG1) |
title_fullStr |
Protein composition of intact and fractionated memberanes isolated from dark and light grown cells of a blue green mutant of Rhodospirillum Rubrum (BG1) |
title_full_unstemmed |
Protein composition of intact and fractionated memberanes isolated from dark and light grown cells of a blue green mutant of Rhodospirillum Rubrum (BG1) |
title_sort |
protein composition of intact and fractionated memberanes isolated from dark and light grown cells of a blue green mutant of rhodospirillum rubrum (bg1) |
url |
http://hdl.handle.net/20.500.12110/paper_00052728_v256_n1_p108_Kerber |
work_keys_str_mv |
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