纯化、鉴定和克隆的胞质天门冬氨酰氨肽酶。
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Wilk年代,Wilk E Magnusson RP
纯化、鉴定和克隆的胞质天门冬氨酰氨肽酶。
J生物化学杂志。1998年6月26日,273 (26):15961 - 70。
- PubMed ID
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9632644 (在PubMed]
- 文摘
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与偏爱n端天门冬氨酰氨肽酶和谷酰基残留物,但不同于谷酰基氨基肽酶(EC 3.4。11.7)纯化从兔大脑细胞溶质附近的同质性。其属性类似于前面描述(凯利,j .酶。Neidle, e . L。Neidle, a (1983) j . Neurochem。40岁,1727 - 1734)。天门冬氨酰氨肽酶对简单aminoacyl-naphthylamide基质几乎没有可检测活动。确定其活动与衬底Asp-Ala-Pro-naphthylamide多余的存在dipeptidyl-peptidase IV (EC 3.4.14.5)。本机酶的分子质量为440 kDa和迁移作为一个乐队的55 SDS-polyacrylamide凝胶电泳后kDa。三个胰蛋白酶的肽的序列被用来屏幕GenBankTM表达序列标签的数据基础。人类和小鼠克隆描述为“类似于酵母空泡的氨肽酶”和包含的全长cdna鉴定和测序。人类的cDNA表达在大肠杆菌。 The amino acid sequence has significant homology to yeast aminopeptidase I, placing it as the first identified mammalian member of the M18 family of metalloproteinases. Homologous sequences in Caenorhabditis elegans and in prokaryotes revealed three conserved histidines, three conserved glutamates and five conserved aspartates. Aspartyl aminopeptidase is found at relatively high levels in all mammalian tissues examined and is likely to play an important role in intracellular protein and peptide metabolism.