Emiliani C, Martino S, Stirling J L, Maras B, Orlacchio A
Dipartimento di Biologia Cellulare e Molecolare, Università degli Studi di Perugia, Italy.
Biochem J. 1995 Jan 15;305 ( Pt 2)(Pt 2):363-6. doi: 10.1042/bj3050363.
Human lysosomal alpha-mannosidase has been purified by a simple and rapid method in sufficient quantities for the analysis of its subunit composition and partial protein sequencing. Analysis of the N-terminal residues of the 30 kDa polypeptide has enabled us to confirm the identity of the recently cloned cDNA that was tentatively identified as that of lysosomal alpha-mannosidase [Nebes and Schmidt (1994) Biochem. Biophys. Res. Commun. 200, 239-245] and to locate the position of this polypeptide within the total deduced amino acid sequence. This finding will therefore provide a firm foundation for the characterization of alpha-mannosidosis mutations.
人溶酶体α-甘露糖苷酶已通过一种简单快速的方法进行了纯化,获得了足够的量用于分析其亚基组成和部分蛋白质测序。对30 kDa多肽的N端残基进行分析,使我们能够确认最近克隆的cDNA的身份,该cDNA最初被暂定鉴定为溶酶体α-甘露糖苷酶的cDNA [内贝斯和施密特(1994年)《生物化学与生物物理研究通讯》200, 239 - 245],并确定该多肽在推导的总氨基酸序列中的位置。因此,这一发现将为α-甘露糖苷贮积症突变的表征提供坚实的基础。