OCCURRENCE AND PURIFICATION OF THE PHOTOACTIVE YELLOW PROTEIN OF ECTOTHIORHODOSPIRA-HALOPHILA (PYP) AND OF IMMUNOLOGICALLY RELATED PROTEINSOF RHODOSPIRILLUM SALEXIGENS AND CHROMATIUM SALEXIGENS AND INTRACELLULAR-LOCALIZATION OF PYP

Authors
THIEMANN B IMHOFF JF
Citation
B. Thiemann et Jf. Imhoff, OCCURRENCE AND PURIFICATION OF THE PHOTOACTIVE YELLOW PROTEIN OF ECTOTHIORHODOSPIRA-HALOPHILA (PYP) AND OF IMMUNOLOGICALLY RELATED PROTEINSOF RHODOSPIRILLUM SALEXIGENS AND CHROMATIUM SALEXIGENS AND INTRACELLULAR-LOCALIZATION OF PYP, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1253(2), 1995, pp. 181-188
Citations number
33
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta. Protein structure and molecular enzymology → ACNP
ISSN journal
01674838
Volume
1253
Issue
2
Year of publication
1995
Pages
181 - 188
Database
ISI
SICI code
0167-4838(1995)1253:2<181:OAPOTP>2.0.ZU;2-A
Abstract
The photoactive yellow protein of Ectothiohodospira halophila (PYP) wa s purified to homogeneity by an advanced method and applied as an affi nity ligand for the isolation of an anti-PYP IgG fraction which was us ed for immunoscreening. The distribution of proteins immunologically r elated to PYP was investigated in protein fractions of 51 strains from 38 species of non-halophilic and halophilic phototrophic and chemotro phic eubacteria and archaeobacteria. Strong immunoreactive bands indic ating the presence of authentic PYP on Western blots (apparent mass 17 .8 kDa) was only found in the strains of E. halophila. Additionally, t wo soluble proteins of Chromatium salexigens and Rhodospirillum salexi gens (apparent molecular masses 16.4 and 19 kDa, respectively) cross-r eacted to approx. 6% and 4%. Analyses of cell fractions of E. halophil a revealed that PYP is a cytoplasmic protein.