| Autor: |
Endo, Toshiya, Oya, Masanao, Kaptein, Robert, Vuister, Geerten W., Kihara, Hiroshi, Mohri, Noriko, Tanaka, Shuji, Ohno, Motonori |
| Zdroj: |
FEBS Letters; March 1988, Vol. 230 Issue: 1-2 p57-60, 4p |
| Abstrakt: |
Proton NMR spectra of a dimeric phospholipase A2from Trimeresurus flavoviridishave been recorded. N‐1 proton resonances of the tryptophan indole rings have been detected and assigned to specific positions, Trp‐3/Trp‐30, Trp‐68 and Trp‐108, by comparing the spectra of the enzyme derivatives with tryptophans oxidized to differing extents. Photo‐CIDNP experiments have revealed that Trp‐68 and Trp‐108 are exposed while Trp‐3 and Trp‐30 are buried in the molecule. This is consistent with the X‐ray crystal structure of a homologous phospholipase A2from Crotalus atroxwhere residues 3 and 30 are located at a dimer interface, but inconsistent with the results of stepwise oxidation of tryptophan residues. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
Plný text