›› 1992, Vol. 10 ›› Issue (3): 187-189.
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Abstract: The horseradish peroxidase labeled affinity purified mice anti-UEA (Urea soluable egg antigen of Schistosoma japonicum) antibody was used in enzyme-linked immunoe ectrotransfer blot (EITB) te monitor the changes after UEA being processed by Mφ.The immune respon-sive peptides were delected in the culture supernatant and homogenate of Mφ pulsed with UEA in vitro (Mφ+).After processing by Mφ the high molecular weight UEA was cleaved into low molecular weight peptides,as shown,by the reactive bands.They markedly differed from that native UEA or trypsin-digested UEA; The bands of Mφ supernatant and homogenate showed similarity with certain quantitative differences.According to the result described above,we considered: 1.UEA could be processed into smaller pieces by Mφ,the style of processing is cleavage.2.The processed peptides might be released to extracellular environment.
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https://www.jsczz.cn/EN/Y1992/V10/I3/187