髓鞘碱性蛋白的adp核糖基化和磷脂囊泡聚集的抑制。

Enzyme & protein Pub Date : 1994-01-01 DOI:10.1159/000474990
C Yamamori, M Terashima, H Ishino, M Shimoyama
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引用次数: 4

摘要

用鸡嗜杂性adp -核糖基转移酶对鸡脑髓鞘碱性蛋白(MBP)的4种同工型进行了adp -核糖基化。21-kD亚型是该转移酶最优先的底物。利用该异构体,NAD的Km值估计为330 μ mol/l, MBP的Km值估计为30 μ mol/l, adp -核糖基化的最佳pH为8.5。adp核糖掺入21-kD MBP的化学计量为3.5 mol adp核糖/mol MBP。我们发现羟胺和l -精氨酸对MBP的adp核糖基化有抑制作用,表明这种修饰可能是由精氨酸残基介导的。鸡adp -核糖基转移酶和霍乱毒素对adp -核糖基化MBP的蛋白水解肽图谱显示出部分不同的放射性活性带。当21-kD MBP被鸡转移酶adp核糖基化后,磷脂囊泡聚集的可能性与adp核糖基化程度成比例地降低。MBP的adp核糖基化可能通过调节髓磷脂在体内的亲和力来控制髓磷脂的稳定,这一可能性需要考虑。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
ADP-ribosylation of myelin basic protein and inhibition of phospholipid vesicle aggregation.

Four isoforms of myelin basic protein (MBP) from chicken brain were ADP-ribosylated by chicken heterophil ADP-ribosyltransferase. The 21-kD isoform was the most preferential substrate of this transferase. With this isoform, the Km values were estimated to be 330 mumol/l for NAD and 30 mumol/l for MBP, and the optimal pH for ADP-ribosylation was 8.5. The stoichiometry of ADP-ribose incorporation into 21-kD MBP was 3.5 mol of ADP-ribose/mol MBP. We found the inhibition of ADP-ribosylation of MBP by hydroxylamine and L-arginine indicating that this modification was likely to be mediated by arginine residues. Proteolytic peptide maps of ADP-ribosylated MBP by chicken ADP-ribosyltransferase and cholera toxin showed partially different radio active bands. When 21-kD MBP was ADP-ribosylated by chicken transferase, the potential for phospholipid vesicle aggregation was reduced in proportion of the degree of ADP-ribosylation. The possibility that ADP-ribosylation of MBP may control stabilization of myelin through regulation of its affinity for phospholipid in vivo would need to be considered.

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