| Literature DB >> 8136350 |
D Douady1, B Rousseau, L Caron.
Abstract
The N-terminus of the major polypeptide component of the light-harvesting complex (LHC) from the brown alga Laminaria saccharina is blocked. Two partial sequences, one near the N-terminus and the other near the C-terminus, have been obtained by chemical cleavage with acetic acid and N-chlorosuccinimide. Four peptides were separated after trypsin digestion of the thylakoid membranes. One fragment is not phosphorylated, is not blocked, and has been sequenced. Purification on a reversed-phase column showed two forms of the LHC protein: the more hydrophobic form appears to be bound to photosystem I. These results are compared with LHC from other Chromophytes and the CAB family of green plants.Entities:
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Year: 1994 PMID: 8136350 DOI: 10.1021/bi00177a004
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162