A locus determining beta-galactosidase activity in the mouse.
A locus determining beta-galactosidase activity in the mouse.
复制标题
决定小鼠β-半乳糖苷酶活性的基因座。
DOI：
--
复制
发表时间：
1974
影响因子：
4.8
通讯作者：
K. Paigen
中科院分区：
文献类型：
--
作者：
J. Felton;M. Meisler;K. Paigen
以C3 H/HeJ为代表的一组近交系小鼠组织中的β-半乳糖苷酶活性是以DBA/2 J为代表的另一组小鼠的两倍。在所有检测的器官中，C3 H/HeJ的较高活性在整个发育过程中表达。活性差异由9号染色体上命名为β-半乳糖苷酶（Bgs）的基因座决定。C3 H/HeJ（Bgsh）和DBA/LiHa（Bgsd）的等位基因表现为加性遗传。对粗匀浆中β-半乳糖苷酶活性的最适pH值、热不稳定性、细胞内位置和分子量的研究表明，仅存在单一酶组分。部分纯化的酶制剂从C3 H/HeJ和DBA/2 J是不可区分的热不稳定性，Km为p-硝基苯基半乳糖苷，和分子量。单一酶组分的存在、可检测的结构差异的缺乏以及Bgs等位基因的加性遗传表明，该位点可能是结构基因复制或控制紧密连锁的β-半乳糖苷酶结构基因的转录或翻译的调控位点。
Abstract A group of inbred mouse strains, typified by C3H/HeJ, have twice as much β-galactosidase activity in their tissues as mice of a second group of strains represented by DBA/2J. In all organs tested, the higher activity in C3H/HeJ is expressed throughout development. The difference in activity is determined by a locus designated β-galactosidase (Bgs) on chromosome 9. The alleles present in C3H/HeJ (Bgsh) and in DBA/LiHa (Bgsd) show additive inheritance. Studies of pH optima, heat lability, intracellular location, and molecular weight of the β-galactosidase activity in crude homogenates suggest that only a single enzyme component is present. Partially purified enzyme preparations from C3H/HeJ and DBA/2J were indistinguishable with respect to heat lability, Km for p-nitrophenylgalactoside, and molecular weight. The presence of a single enzyme component, the absence of detectable structural differences, and the additive inheritance of Bgs alleles suggest that this locus may be either a structural gene duplication or a regulatory site controlling the transcription or translation of a closely linked β-galactosidase structural gene.