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. 2014 Feb 18;2014:341270. doi: 10.1155/2014/341270

Figure 1.

Figure 1

Purification and chemical modification of secretory phospholipase A2 (sPLA2). A fractionation of the whole venom was performed by reverse-phase HPLC (C5 column, 0.10 cm × 25 cm) using a nonlinear concentration gradient of buffer to obtain a high-purity protein. (a) shows a comparative profile of native sPLA2, sPLA2 : Q, and sPLA2 : Qn when subjected to reverse-phase HPLC. (b) shows the MALDI-TOF mass spectrometry analysis of native sPLA2 and sPLA2 : Qn, indicating the difference in the molecular mass corresponding to one molecule of bound quercitrin.