ASIA unversity:Item 310904400/4518
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    题名: Structural organization of apolipoprotein B-100 of human plasma low density lipoproteins. Comparison to B-48 of chylomicrons and very low density lipoproteins
    作者: Cardin AD;Price CA;Hirose N;Krivanek M;Blankenship DT;Chao J;Mao SJT
    贡献者: Department of Biotechnology
    日期: 1986-12
    上传时间: 2009-11-26 01:43:32 (UTC+0)
    出版者: Asia University
    摘要: The present study characterizes the substructural organization of apolipoprotein B-100 (B-100) of human plasma low density lipoproteins (LDL) and its relation to B-74 and B-26 of LDL and B-48 of chylomicrons and very low density lipoproteins. LDL were digested with human kallikrein and thrombin to yield two major fragments: K1 (Mr 410,000) and K2 (Mr 145,000) and T1 (Mr 385,000) and T2 (Mr 170,000), respectively. The antigenic sequences, Mr, and amino acid compositions of K1 and K2 were identical to those of plasma B-74 and B-26; B-26 and K2 had identical NH2-terminal sequences and correspond to the NH2-terminal region of B-100. K1 was further degraded by kallikrein to give K3 (Mr 235,000) and K4 (Mr 170,000); these peptides correspond immunochemically to two newly discovered plasma LDL peptides B-44 and B-30 and are assigned as complementary fragments of B-74. The thrombin cleavage fragments, T1 and T2, did not correspond to B-74 and B-26. Neither kallikrein nor thrombin generated a fragment from B-100 corresponding to B-48 in chylomicrons. However, B-48 showed antigenic homology with B-26 and to the of B-74 adjoining B-26, indicating that its structure is represented in the NH2-terminal half of B-100. The structural studies further clarify the relatedness among the B-100, B-74, B-26, and B-48 polypeptides and should now make possible the delineation of the functional domains mediating the interactions of apolipoprotein B in the circulation and arterial wall.
    關聯: The Journal of Biological Chemistry 261(35):16744-8
    显示于类别:[生物科技學系] 期刊論文

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