ISOLATION, AMINO ACID COMPOSITION AND SOME PHYSICO-CHEMICAL PROPERTIES OF THE PROTEIN DEUTERIO-PHYCOCYANIN
The isolation and purificntion of a fully deuteriated protein, deuterio- phycocyanin, from blue-green algae grown autotrophically in 99.8% D/sub 2/O is described. Sedimentation behavior in the ultracentrifuge shows the protein to be a system of reversibly interacting components. The amino acid compositions of ordinary and deuterio-phycocyanin isolated from Plectonema calothricoides were establishcd and it appears that the amino acid compositions are identical within experimental error. Ordinary and deuterio-phycocyanin therefore probably differ only in isotopic composition. Thermal denaturation of ordinary and deuterio- phycocyanin, both dissolved in H/sub 2/O was studied by measuring the quenching of fluorescence. Deuteriophycocyanin undergoes thermal denaturation at a temperature 5 deg lower than ordinary phycocyanin. Since the two proteins appear to differ primarily in the isotopic composition of the non-polar side chains, differences in denaturation behavior are probably to be ascribed to differences in hydrophobic bonding. (auth)
- Research Organization:
- Argonne National Lab., Ill.
- Sponsoring Organization:
- USDOE
- NSA Number:
- NSA-17-012310
- OSTI ID:
- 4707882
- Report Number(s):
- TID-17096; 0002-7863
- Journal Information:
- Journal of the American Chemical Society (U.S.), Vol. Vol: 85; Other Information: TID-17096. Orig. Receipt Date: 31-DEC-63
- Country of Publication:
- Country unknown/Code not available
- Language:
- English
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