Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1976-7-6
pubmed:abstractText
The chromophore of C-phycocyanin, phycocyanobilin, was cleaved from the protein with methanol, concentrated hydrochloric acid, or subtilisin BPN'. The pigments obtained were converted to their dimethyl esters and purified by preparative high pressure liquid chromatography and examined for purity by analytical high pressure chromatography on silica gel. They were characterized by proton transfer and electron impact mass spectroscopy. The principal product obtained by the three cleavage procedures was phycocyanobilin. Methanol and hydrochloric acid adducts of phycocyanobilin were obtained with methanol and concentrated hydrochloric acid cleavages, respectively. Methanol adduct formation of phycocyanobilin can occur subsequent to cleavage and requires acid catalysis. No adduct formation was observed with mesobiliverdin under similar conditions. These results and mass spectral data support the conclusion that adduct formation takes place at the exocyclic olefin linkage of ring A in phycocyanobilin. The ease of co-valent adduct formation strongly suggests that the ethylidene side chain is an important binding site of phycocyanobilin to the polypeptide chain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
251
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2405-11
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Cleavage of phycocyanobilin from C-phycocyanin. Separation and mass spectral identification of the products.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.