| Chuang MT |
------>authors3_c=??? ------>paper_class1=1 ------>Impact_Factor=2.701 ------>paper_class3=2 ------>paper_class2=1 ------>vol=28 ------>confirm_bywho=hsu0320 ------>insert_bywho=wchou ------>Jurnal_Rank=32.7 ------>authors4_c= ------>comm_author=1 ------>patent_EDate=None ------>authors5_c= ------>publish_day=1 ------>paper_class2Letter=None ------>page2=1316 ------>medlineContent= ------>unit=G0200 ------>insert_date=20071107 ------>iam=3 ------>update_date=None ------>author=??? ------>change_event=4 ------>ISSN= ------>authors_c=??? ------>score=500 ------>journal_name=Peptides ------>paper_name=Ancordin, the major rhizome protein of madeira-vine, with trypsin inhibitory and stimulatory activities in nitric oxide productions ------>confirm_date=20071220 ------>tch_id=089063 ------>pmid=17499881 ------>page1=1311 ------>fullAbstract=Anredera cordifolia (Ten.) Steenis, or the synonymous name of Boussingaultia baselloides or Boussingaultia gracilis var. pseudobaselloides, is a South American species of ornamental succulent vine, commonly known as the madeira-vine. The fresh leaves of madeira-vine are frequently used as vegetables. A. cordifolia is an evergreen climber that grows from fleshy rhizomes. The rhizome contained one major (23kDa) protein band under non-reducing condition in the SDS-PAGE. The first 15 amino acids in the N-terminal region of the major protein band (23kDa), named tentatively ancordin, were KDDLLVLDIGGNPVV which were highly homologous to sequences of winged bean seed protein ws-1, Medicago truncatula proteinase inhibitor, soybean trypsin inhibitor, and sporamin. By using activity stains, the ancordin showed trypsin inhibitory activity in the SDS-PAGE gel which was found not only in rhizomes but also in aerial tubers, but few in fresh leaves. The crude extracts from rhizomes of madeira-vine were directly loaded onto trypsin-Sepharose 4B affinity column. After washing with 100mM Tris-HCl buffer (pH 7.9) containing 100mM NaCl, the ancordin was eluted directly by 0.2M KC1-HC1 buffer (pH 2.0). In calculation, the purified protein exhibited 0.0428mug trypsin inhibition/mug ancordin (corresponding to 0.53 unit of TPCK-treated trypsin inhibited/mug ancordin). The purified ancordin was used to evaluate the nitric oxide productions in RAW264.7 cells in the presence of polymyxin B (poly B, 50microg/ml) to eliminate the lipopolysaccharide (LPS) contaminations. It was found that ancordin (1.25-5microg/ml) could dose-dependently (R=0.954) stimulate the nitric oxide (NO) productions (expressed as nitrite concentrations) in RAW264.7 cells without significant cytotoxicity, and kept the similar effects in NO production in 6.25microg/ml ancordin. ------>tmu_sno=None ------>sno=16127 ------>authors2=Lin YS ------>authors3=Hou WC ------>authors4= ------>authors5= ------>authors6= ------>authors6_c= ------>authors=Chuang MT ------>delete_flag=0 ------>SCI_JNo=None ------>authors2_c=??? ------>publish_area=0 ------>updateTitle=Ancordin, the major rhizome protein of madeira-vine, with trypsin inhibitory and stimulatory activities in nitric oxide productions. ------>language=2 ------>check_flag=None ------>submit_date=None ------>country=None ------>no= ------>patent_SDate=None ------>update_bywho=None ------>publish_year=2007 ------>submit_flag=None ------>publish_month=1 |