Accession Number : AD0620716

Title :   PURIFICATION AND N-TERMINAL ANALYSES OF ALGAL BILIPROTEINS,

Corporate Author : UNIVERSITY COLL GALWAY (IRELAND)

Personal Author(s) : Carra,P. O.

Report Date : 19 MAY 1964

Pagination or Media Count : 6

Abstract : R-, B- and C-phycoerythrins and R- and C-phycocyanins were isolated and purified on a preparative scale by calcium phosphate chromatography, ammonium sulphate fractionation and crystallization. The N-terminal residues of these biliproteins were analysed. Methionine is the only N-terminal residue of all the phycoerythrins, there being about 14 N-terminal residues per molecule of Rand B-phycoerythrins (mol.wt. 290 000) and about 8 per molecule of C-phycoerythrin (mol.wt. 226 000). Threonine (1 residue) is N-terminal in C-phycocyanin (mol.wt. 138 000), and both threonine (about 1.3 residues) and methionine (5 residues) are N-terminal in R-phycocyanin (mol.wt. 273 000). Results suggest that the apoproteins of the various phycoerythrins are closely related, whereas C-phycocyanin has quite a different gross structure, and that R-phycocyanin contains two types of sub-unit, one related to C-phycocyanin and the other to the phycoerythrins. (Author)

Descriptors :   (*ALGAE, PROTEINS), (*PROTEINS, MOLECULAR STRUCTURE), (*ORGANIC PIGMENTS, MOLECULAR STRUCTURE), PURIFICATION, CHEMICAL ANALYSIS, CHROMATOGRAPHIC ANALYSIS, CRYSTALLIZATION, AMINO ACIDS, METHIONINE, IRELAND

Distribution Statement : APPROVED FOR PUBLIC RELEASE