An Evaluation of 3-Rhamnosylquercetin, a Glycosylated Form of Quercetin, against the Myotoxic and Edematogenic Effects of sPLA₂ from Crotalus durissus terrificus

Figure 2

The far-UV (ultraviolet) CD spectrum of proteins can reveal important characteristics of their secondary structure. (a) shows the results of CD spectra from native sPLA₂, sPLA₂ : Q, and sPLA₂ : Qn. Data from 185–280 nm are shown. The CD spectra are expressed in theta machine units in millidegrees. The near-UV CD spectrum (>250 nm) of proteins provides information on the tertiary structure. The signals obtained in the 250–300 nm region are caused by the absorption, dipole orientation, and the nature of the surrounding environment around the phenylalanine, tyrosine, cysteine (or S-S disulfide bridges), and tryptophan amino acids. (b) shows the near-UV CD spectrum of the native sPLA₂, sPLA₂ : Q, and sPLA₂ : Qn.

(a)

(b)