1790 CHEMISTRY OF CHLOKOPLAST PIGMENTS CHAP. 37B 



Haxo, O'hEocha and Strout (1954) found typical "P-phycoerythrin," 

 with peaks at 497, 537 and 566 mn, in Rhodymenia palmata and Polyneura 

 latissima, and typical "C-phycoerythrin," with a single peak at 560 m/x, in 

 Phormidium persicinum, Ph. fragile, and Nostoc. On the other hand, Ph. 

 ectocarpi yielded a phycoerythrin with only two peaks, at 542 and 56() m/x. 

 In Bangiales, such as Prophyra tenera or P. perforata, they found a phyco-> 

 erythrin with peaks at 497 and 566 mn, but with no definite middle peak. 

 Phycoerythrin from another of the Bangiales, Porphyridium cruentum, 

 had only one broad band, at 545 mu, and three bands in the ultraviolet, at 

 368, 306 and 276 m/t, the second of which is not present in R-phycoery- 

 thrin. 



Krasno^'sky, Evstigneev, Brin and Gavrilova (1952) found that phy- 

 coerythrin can be extracted from CaUilhamnion rybosum more conveniently 

 than from Ceramium. They purified the extracted pigment by chromatog- 

 raphy on a tricalcium phosphate column. Developing with 0.15 M di- 

 sodium phosphate permitted complete separation from phycocyanin. The 

 product, extracted into 0.15 M Na2HP04, showed two protein fractions 

 in the ultracentrifuge, Avith M = 300,000 and M ^ 50,000, respectively. 

 The phycoerythrin solution was found to be photochemically stable against 

 oxidation by air, as well as against reduction by ascorbic acid. It therefore 

 did not sensitize the reduction of riboflavin or safranin by ascorbic acid. 

 (These results, belonging in Chapter 35, were not mentioned there.) Pho- 

 toxidation was accelerated by dioxane or pyridine, and seemed to in\-olve a 

 partial separation of the chromophore from the protein (drop of absorption 

 at 565 and 540 m/x, preservation of the 495 m/x peak). 



This observation may be interesting from the point of view of a search 

 for better methods of separation of erythrobilin from its associated protein 

 — a most important hurdle in the study of these pigments. The methods 

 in use at present — hydrolysis with hot hydrochloric acid or alkaline hy- 

 drolysis (Bannister 1954) — destroy a large part of the chromophore while 

 prying it off the protein. 



Bibliography to Chapter 37B 

 Chemistry of Chloroplast Pigments 



1939 Godnev, T. N., I'chenyje Zapiski Beloniss. Univ. (Chem. Ser.), 1939, No. 1, 

 15. 



1943 Noack, K., Biochem. Z., 316, 166. 



1944 Fischer, H., and Pfeiffei'. H., Ann. Chem. Ju.^lus Liehigs, 555, 94. 

 Godnev, T. N., and Kalishevish, S. V., Trudy Inst. Fisiol, Rmtmij,, 1944, 



No. 2, 160. 



