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丝状线虫指状丝虫表面抗原的分离与分析。

Isolation and analysis of surface antigens of filarial nematode Setaria digitata.

作者信息

Bright J J, Raj R K

机构信息

Department of Biochemistry, University of Kerala, Kariavattom, Thiruvananthapuram, India.

出版信息

Indian J Exp Biol. 1991 Aug;29(8):725-9.

PMID:1769714
Abstract

Surface antigens of adult filarial parasite S. digitata was isolated by employing techniques from manual dissection to treatment with detergents. Among the surface antigen preparations (SAPs), the activities of marker enzymes such as alkaline phosphatase, adenosine triphosphatase and 5' nucleotidase were higher with that isolated by triton X-100 technique (SAP2). On SDS-PAGE, the SAP2 has three major proteins with molecular weights 17, 29 and 36 KD which were consistent with the PBS soluble cuticular proteins (SAP1). Besides these, few other minor protein bands were also observed with the other SAPs. All SAPs were antigenic and showed positive reaction against antiserum to SAP2, and the results confirmed the SAP2 as a better preparation. The release of 29 KD surface protein during in vitro culture of adult parasite and its cross-reactivity with antiserum to surface antigens revealed the possible natural shedding of surface molecules into the host system.

摘要

通过采用从手工解剖到用去污剂处理的技术,分离出成年丝状寄生虫指状丝虫的表面抗原。在表面抗原制剂(SAPs)中,诸如碱性磷酸酶、三磷酸腺苷酶和5'核苷酸酶等标记酶的活性在通过曲拉通X-100技术分离的制剂(SAP2)中更高。在SDS-PAGE上,SAP2有三种主要蛋白质,分子量分别为17、29和36千道尔顿,这与PBS可溶性表皮蛋白(SAP1)一致。除此之外,在其他SAPs中也观察到一些其他较小的蛋白条带。所有SAPs都具有抗原性,并且对SAP2抗血清呈阳性反应,结果证实SAP2是一种更好的制剂。成年寄生虫体外培养期间29千道尔顿表面蛋白的释放及其与表面抗原抗血清的交叉反应揭示了表面分子可能自然脱落到宿主系统中。

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