Abstract:
:Reaction center of chromatophores of Rhodospirillum rubrum consists of three kinds of protein, H-, M-, and L-subunit, and is bound with many other kinds of protein to form a larger protein complex (PRU; photoreaction unit), which contains all the bacteriochlorophyll. In the present study, purified PRU was dissociated in a stepwise manner in the presence of various mixtures of lithium dodecyl sulfate, sodium cholate and/or sodium deoxycholate, and separated into five, smaller protein complexes (PL1, PL2, PL3, PL4, and PL4') by high-speed molecular-sieve chromatography. The protein complexes were analyzed for molecular mass (Mm), protein composition, and molecular weights of the constituent proteins by the chromatography described above and by lithium or sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The results suggest that PRU consisted of 1 molecule each of 40K, 39K, 31K (H-subunit), 25K (M-subunit), and 22K (L-subunit), about 12 molecules each of 12K (light-harvesting bacteriochlorophyll-protein) and 11K, and about 6 molecules each of 10K and 9K (the protein nomenclature refers to the apparent molecular weights); the measured and calculated Mm values were 650K and 547K, respectively. The compositions of the other protein complexes were as follows. PL1 = PRU-10K-9K (measured & calculated Mm, 520K & 409K); PL2 = PL1-39K (340K & 267K); PL3 = PL2-40K (160K & 147K); PL4 = PL3-31K-25K (90K & 82K); PL4' = 31K + 25K + 22K (inactivated reaction center) (90K & 78K). The molar ratios of 12K and 11K to 25K were lower in the dissociated protein complexes than in PRU, and they differed from one complex to another. The locations of the constituent proteins in PRU are discussed.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Tanaka K,Kakuno T,Yamashita J,Horio Tdoi
10.1093/oxfordjournals.jbchem.a134534subject
Has Abstractpub_date
1983-12-01 00:00:00pages
1815-26issue
6eissn
0021-924Xissn
1756-2651journal_volume
94pub_type
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