STRUCTURE-FUNCTION RELATIONSHIPS OF LYSOSOMAL ENZYMES

β-氨基己糖苷酶已经成为一种理解 溶酶体酶生物学。为了更深入地了解 Hexosamidase系统，我们已经分离了覆盖 编码该酶的阿尔法链的整个基因。这些克隆人已经 限制性内切酶图谱、Southern blotting和DNA 测序。阿尔法链基因跨越35千个碱基的dna并且是分裂的。 分成14个外显子。内含子的位置与潜在蛋白质相匹配 加工位点，表明基因结构与蛋白质相关 结构。该基因的启动子区域含有常规的“TATA” 和“CAAT”图案。我们还分离了编码基因的cdna和基因组克隆。 氨基己糖苷酶的β链。这些克隆的序列分析 表明与阿尔法链具有广泛的结构同源性 在两个亚基的氨基末端有显著差异。

Beta-hexosaminidase has become a paradigm for the understanding of lysosomal enzyme biology. In order to gain further insight into the hexosaminidase system, we have isolated human genomic clones covering the entire gene encoding the alpha chain of the enzyme. These clones have been characterized by restriction mapping, Southern blotting and DNA sequencing. The alpha chain gene spans 35 kilobases of DNA and is split into 14 exons. The position of introns matches potential protein processing sites, indicating a correlation of gene structure with protein structure. The promoter region of this gene contains conventional "TATA" and "CAAT" motifs. We have also isolated cDNA and genomic clones encoding the beta chain of hexosaminidase. Sequence analysis of these clones indicate extensive structural homology with the alpha chain with significant differences at the amino-termini of the two subunits.