A novel serine protease with human fibrino(geno)lytic activities from Artocarpus heterophyllus latex

作者：Siritapetawee Jaruwan^*; Thumanu Kanjana; Sojikul Punchapat; Thammasirirak Sompong

来源：Biochimica et Biophysica Acta-Proteins and Proteomics, 2012, 1824(7): 907-912.

DOI：10.1016/j.bbapap.2012.05.002

• Artocarpus heterophyllus
• Jackfruit
• Latex
• Serine protease

A protease was isolated and purified from Artocarpus heterophyllus (jackfruit) latex and designated as a 48-kDa antimicrobial protease (AMP48) in a previous publication. In this work, the enzyme was characterized for more biochemical and medicinal properties. Enzyme activity of AMP48 was strongly inhibited by phenylmethanesulfonyl fluoride and soybean trypsin inhibitor, indicating that the enzyme was a plant serine protease. The N-terminal amino acid sequences (A-Q-E-G-G-K-D-D-D-G-G) of AMP48 had no sequence similarity matches with any sequence databases of BLAST search and other plant serine protease. The secondary structure of this enzyme was composed of high alpha-helix (51%) and low beta-sheet (9%). AMP48 had fibrinogenolytic activity with maximal activity between 55 and 60 degrees C at pH 8. The enzyme efficiently hydrolyzed alpha followed by partially hydrolyzed beta and gamma subunits of human fibrinogen. In addition, the fibrinolytic activity was observed through the degradation products by SDS-PAGE and emphasized its activity by monitoring the alteration of secondary structure of fibrin clot after enzyme digestion using ATR-FTIR spectroscopy. This study presented the potential role to use AMP48 as antithrombotic for treatment thromboembolic disorders such as strokes, pulmonary emboli and deep vein thrombosis.

• 出版日期2012-7