Characterization of phycoerythrin from a Cryptomonas sp. |
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| Authors: | A. N. Glazer Germaine Cohen-Bazire R. Y. Stanier |
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| Affiliation: | (1) Department of Bacteriology and Immunology, University of California, 94720 Berkeley, California, USA;(2) Present address: Department of Biological Chemistry, UCLA School of Medicine, 90024 Los Angeles, California, USA |
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| Abstract: | Summary Two closely similar phycoerythrins were purified from Cryptomonas sp. The two proteins were indistinguishable with respect to native molecular weight, subunit structure, photolability and immunological specificity, and differed only in their isoelectric points (pH 5.74 and 6.35), as determined by isoelectric focussing in polyacrylamide gels. Each protein consisted of two unequal subunits,  (mol. wt. 11,800) and  (mol. wt. 19,000), and each subunit contained covalently bound chromophore. In contrast to the blue-green and red algal phycoerythrins studied thus far, the Cryptomonas sp. phycoerythrins are extremely photolabile; exposure of the purified proteins to relatively short periods of intense illumination with visible light produces a marked decrease in fluorescence and in absorbance at 567 m .Abbreviation used SDS sodium dodecyl sulfate |
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