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Chapter 44,288

Selective labelling of the beta-subunit of L-phenylalanyl-tRNA synthetase from E. coli with N-bromoacetyl-L-phenylalanyl-tRNA Phe

Bartmann, P.; Hanke, T.; Hammer-Raber, B.; Holler, E.

Biochemical and Biophysical Research Communications 60(2): 743-747

1974

ISSN/ISBN: 0006-291X
PMID: 4607775
DOI: 10.1016/0006-291x(74)90303-9
Accession: 044287660
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L-Phenylalanyl-t Rna synthetase has been reacted with N-bromoacetyl-[14C]Phe-t RNAPhe to yield covalently linked enzyme-N-acetyl-[14C]Phe-t RNAPhe. The labelled enzyme was dissociated in the presence of 4M guanidinium chloride and the subunits subsequently separated by gel chromatography. The elution pattern is indicative of covalent binding of the t Rna to the β-subunit of the enzyme.

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Related References

Rauhut, R.; Gabius, H.J.; Engelhardt, R. 1985: Archaebacterial phenylalanyl-tRNA synthetase. Accuracy of the phenylalanyl-tRNA synthetase from the archaebacterium Methanosarcina barkeri, Zn(II)-dependent synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate, and immunological relationship of phenylalanyl-tRNA synthetases from different urkingdoms Journal of Biological Chemistry 260: 2-7
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