Jacobson L A, Jen-Jacobson L, Hawdon J M, Owens G P, Bolanowski M A, Emmons S W, Shah M V, Pollock R A, Conklin D S
Department of Biological Sciences, University of Pittsburgh, Pennsylvania 15260.
Genetics. 1988 Jun;119(2):355-63. doi: 10.1093/genetics/119.2.355.
Mutants of Caenorhabditis elegans having about 10% of wild-type activity of the aspartyl protease cathepsin D have been isolated by screening. Mutant homozygotes have normal growth rates and no obvious morphological or developmental abnormalities. The mutant gene (cad-1) has been mapped to the right extremity of linkage group II. Heterozygous animals (cad-1/+) show intermediate enzyme levels and animals heterozygous for chromosomal deficiencies of the right extremity of linkage group II have 50% of wild-type activity. Cathepsin D purified from a mutant strain has a lower activity per unit mass of pure enzyme. These data suggest that cad-1 is a structural gene for cathepsin D.
通过筛选，已分离出具有约10%野生型天冬氨酸蛋白酶组织蛋白酶D活性的秀丽隐杆线虫突变体。突变纯合子具有正常的生长速率，且无明显的形态或发育异常。突变基因（cad-1）已被定位到连锁群II的右端。杂合动物（cad-1/+）显示出中等酶水平，而连锁群II右端染色体缺失的杂合动物具有50%的野生型活性。从突变菌株中纯化的组织蛋白酶D每单位质量纯酶的活性较低。这些数据表明cad-1是组织蛋白酶D的一个结构基因。
