Gamo T
Biochem Genet. 1982 Feb;20(1-2):165-77. doi: 10.1007/BF00484944.
A variant sericin polypeptide originally found by acid gel electrophoresis in the Nd-s mutant strain of the silkworm, Bombyx mori, has been analyzed genetically. The variant polypeptide (called S-2v) is encoded by a gene which behaves as a codominant allele of the gene encoding the standard S-2 sericin polypeptide. Linkage analysis locates these alleles at 0.0 map unit on chromosome 11. SDS-polyacrylamide gel electrophoresis shows that the molecular weight of the S-2v variant polypeptide is lower by approximately 62,500 than that of the S-2 polypeptide. Amino acid analysis indicates that the two sericin polypeptides have similar compositions. These results are consistent with the idea that the variant allele arose by deletion within the S-2 coding sequence in the Src-2 gene locus as the result of unequal recombination.
一种最初通过酸性凝胶电泳在家蚕（Bombyx mori）的Nd-s突变株中发现的变异丝胶蛋白多肽已进行了遗传分析。该变异多肽（称为S-2v）由一个基因编码，该基因表现为编码标准S-2丝胶蛋白多肽的基因的共显性等位基因。连锁分析将这些等位基因定位在第11号染色体上0.0个图距单位处。SDS-聚丙烯酰胺凝胶电泳显示，S-2v变异多肽的分子量比S-2多肽低约62,500。氨基酸分析表明，这两种丝胶蛋白多肽具有相似的组成。这些结果与以下观点一致，即变异等位基因是由于Src-2基因座中S-2编码序列内的不等位重组导致缺失而产生的。
