Neutrophil elastase inhibitor purification strategy from cowpea seeds

• DOI: 10.1371/journal.pone.0223713
• Publication Date: 2019-10-10T18:51:32Z
• Authors: Graziele Cristina...; Adriana Feliciano...; Flavia Ribeiro Sa...; Livia de Moraes B...; Gabriel Capella M...; Sergio Daishi Sasaki
• Keywords: Molecular mass; Serine Proteinase Inhibitors; Pancreatic elastase; Neutrophil elastase

Serine proteases and its inhibitors are involved in physiological process deregulation lead to various diseases like Chronic Obstructive Pulmonary Disease (COPD), pulmonary emphysema, skin diseases, atherosclerosis, coagulation cancer, inflammatory neuronal disorders other diseases. protease have been described many species, as well plants, including cowpea beans (Vigna unguiculata (L.) Walp). Here, we purified characterized a inhibitor, named VuEI elastase inhibitor), from Vigna unguiculata, with inhibitory activity against HNE (human neutrophil elastase) chymotrypsin but has no trypsin thrombin. was obtained by alkaline protein extraction followed three different chromatographic steps sequence. First, an ion exchange chromatography using Hitrap Q column employed, two reversed-phase Source15RPC ACE18 columns. The molecular mass of estimated 10.99 kDa MALDI-TOF spectrometry. dissociation constant (Ki) 9 pM. These data indicate that is potent inhibitor human elastase, besides inhibit chymotrypsin.