Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
1976-3-11
pubmed:abstractText
Pigment-protein complexes excreted from three bacteriochlorophyll-less mutants (mutants 8, 8-29, and 8-47) of Rhodopseudomonas sphaeroides have been isolated and purified. In the absence of detergents the complexes remained in an aggregated state, but were disaggregated by 0.2% Triron X-100. Sepharose 6B gel filtration indicated that the disaggregated complex from each of the mutants had a particle weight of about 165000, and contained 30 +/- 3% protein. This complex was further dissociated by 1% sodium dodecyl sulfate. Sephadex G-100 gel filtration now indicated that the majority of the protein was present as a small polypeptide with a molecular weight of about 9000. The pigment-protein complex from one of the mutants was treated with a bacteriochlorophyll extract. The bacteriochlorophyll was converted to bacteriopheophytin and became bound to the protein, replacing the endogenous tetrapyrrole (a bacteriocholorophyll precursor). The red absorption maximum of the bacteriopheophytin was shifted during this process to 840-865 nm. These properties are consistent with the possibility that the pigment-protein complexes contain a protein normally associated with light-harvesting bacteriochlorophyll in the wide-type strain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5554-61
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
The nature of a pgiment-protein complex excreted from mutants of Rhodopseudomonas sphaeroides.
pubmed:publicationType
Journal Article