Premium
Purification and molecular properties of 3 polypeptides released from a highly active O 2 ‐evolving photosystem‐II preparation by Tris‐treatment
Author(s) -
Yamamoto Yasusi,
Shimada Shoko,
Mitsuo Nishimura
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80340-8
Subject(s) - tris , photosystem ii , isoelectric point , isoelectric focusing , histidine , chemistry , methionine , photosystem , amino acid , biochemistry , amino acid residue , chromatography , peptide sequence , enzyme , photosynthesis , gene
Tris‐treatment of a highly active O 2 ‐evolving photosystem‐II preparation induced release of 3 polypeptides ( M r 33 000, 24 000 and 18 000), concomitant with inhibition of O 2 evolution [FEBS Lett. (1981)_133. 265‐268]. The 3 polypeptides were purified with the use of electrofocusing. Isoelectric points of the proteins were 5.1, 6.5 and 9.2 in order of decreasing M r value. Only a trace amount of histidine, cystein and methionine were detected in these proteins. Based on the amino acid compositions, polarity indexes of the proteins were calculated to be 47–49%, suggesting the 3 proteins to be hydrophilic.