
Striking differences of physical properties for two different phenylalanyl‐tRNA synthetases in Cyanophora paradoxa
Author(s) -
Rauhut Reinhard,
Gabius HansJoachim,
Cramer Friedrich
Publication year - 1985
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1985.tb00662.x
Subject(s) - biology , zoology , chemistry
Extracts of Cyanophora paradoxa contain 2 activities for phenylalanyl‐tRNA synthetase (PRS), when assayed with yeast and eubacterial tRNA as substrate. These enzymes can be separated by salting‐out chromatography. Subsequent gel filtration revealed a striking difference in M r between the 2 enzymes. Whereas the M r of the enzyme aminoacylating yeast tRNA is 260 000, typical for PRS from lower eukaryotic organisms, the second enzyme has a unique M r of 80 000. It aminoacylates eubacterial tRNA, but shows no immunological relationship to the corresponding enzyme from Escherichia coli .