Isolation and localization of XXXX in phycobiliproteins from the cyanobacterium Mastigocladus laminosus.

@entity35139 @entity535 @entity2734 @entity8776 @entity70977 @entity6702
The occurrence of post-translationally methylated @entity2734 residues in beta AP from @entity6702 , @entity35139 and Porphyridium cruentum has recently been reported (Klotz, A.V., Leary, J.A. _ Glazer, A.N. (1986) J. Biol. Chem. 261, 15891-15894). We reinvestigated the @entity535 compositions of all phycobiliproteins from Mastigocladus laminosus. During total hydrolysis of beta AP, beta 16.2 and beta PC one mol @entity8776 per mol protein was released. These proteins were chemically and enzymatically fragmented and the sequences of the fragments containing the modified @entity2734 residue were determined by automated Edman degradation. Residues beta AP72, beta 16.2 72 and beta PC 72 were identified as @entity70977 . This derivative of @entity2734 was also found at a homologous position in beta PE of Calothrix. In the x-ray structure model of C-phycocyanin (PC) the residue beta PC 72 points towards the chromophore beta 84, presumably having an effect on the spectroscopic characteristics of this light harvesting pigment protein complex.
