In:
FEBS Letters, Wiley, Vol. 304, No. 2-3 ( 1992-06-15), p. 249-251
Abstract:
Ricin A‐chain, an N ‐glycosidase that attacks 28S rRNA at a highly conserved adenine residue, has a unique tryptophan (Trp‐211) in the putative active site cleft. Fluorescence spectroscopy revealed that specific binding of adenine to the A‐chain caused a large enhancement of Trp‐211 fluorescence (70%) and a concomitant red shift of the emission spectrum (8 nm). A Scatchard plot of the fluorescence enhancement data was not linear, indicating that the environment of Trp‐211 was altered by heterogeneous binding of adenines. These results, taken together with the protective effect of adenine on the ribosome‐inactivation by ricin A‐chain, suggest that at least two adenines bind to the active site cleft.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(92)80630-Y
Language:
English
Publisher:
Wiley
Publication Date:
1992
detail.hit.zdb_id:
1460391-3
SSG:
12
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