Ho, C.L., Lin, Y.L., Chen, W.C., Yu, H.M., Wang, K.T., Hwang, L.L., and Chen, C.T. |
------>authors3_c=None ------>paper_class1=1 ------>Impact_Factor=None ------>paper_class3=2 ------>paper_class2=1 ------>vol=33 ------>confirm_bywho=wslee ------>insert_bywho=llhwang ------>Jurnal_Rank=None ------>authors4_c=None ------>comm_author= ------>patent_EDate=None ------>authors5_c=None ------>publish_day=None ------>paper_class2Letter=None ------>page2=1451 ------>medlineContent= ------>unit=000 ------>insert_date=20000626 ------>iam=7 ------>update_date= ------>author=??? ------>change_event=5 ------>ISSN=None ------>authors_c=None ------>score=500 ------>journal_name=Toxicon ------>paper_name=Immunogenicity of mastoparan B, a cationic tetradecapeptide isolated from the hornet (Vespa basalis) venom, and its structural requirements. ------>confirm_date=20020507 ------>tch_id=089017 ------>pmid=8744984 ------>page1=1443 ------>fullAbstract=Mastoparan B (MP-B) is a cationic tetradecapeptide (LKLKSIVSWAKKVL-CONH2, mol. wt 1611) isolated from the black-bellied hornet (Vespa basalis) venom. The small peptide itself was capable of inducing antibodies without prior conjugation to a protein carrier in rabbits and mice. The mouse antibody was found to be of IgG1 isotype with kappa-type light chain. The peptide antigen was able to form insoluble complexes with the specific antibody, suggesting that MP-B possessed more than one epitope in its molecule. The finding that MP-B was able to bind with both mouse and rabbit antibodies in sandwich ELISA supports this contention. Synthetic MP-B analogues in which lysine at position 2, 4, 11 or 12 was replaced by neutral amino acids such as asparagine or leucine showed a significant decrease in their antibody-binding activities. Substitution of lysine at position 4 (Lys4) caused the most marked inhibition in its binding activity. However, replacing tryptophan at position 9 by tyrosine caused a relatively small reduction in its binding activity. Replacing both Lys2,4 by asparagine or removing Lys-containing segments at amino or carboxyl terminus in MP-B sequence caused a remarkable decrease in the antibody-binding and immunogenic activities of the peptide. The Lys residues located at amino and carboxyl terminal segments of MP-B, especially Lys4, appear to play a critical role in the binding interaction and the immunogenicity of the peptide. ------>tmu_sno=None ------>sno=2102 ------>authors2=None ------>authors3=None ------>authors4=None ------>authors5=None ------>authors6=None ------>authors6_c=None ------>authors=Ho, C.L., Lin, Y.L., Chen, W.C., Yu, H.M., Wang, K.T., Hwang, L.L., and Chen, C.T. ------>delete_flag=0 ------>SCI_JNo=None ------>authors2_c=None ------>publish_area=None ------>updateTitle=Immunogenicity of mastoparan B, a cationic tetradecapeptide isolated from the hornet (Vespa basalis) venom, and its structural requirements. ------>language=2 ------>check_flag= ------>submit_date= ------>country=None ------>no= ------>patent_SDate=None ------>update_bywho= ------>publish_year=1995 ------>submit_flag= ------>publish_month=None |