非洲爪蟾中小卵黄脂磷蛋白亚基在卵黄蛋白原前体中的定位。

Placement of small lipovitellin subunits within the vitellogenin precursor in Xenopus laevis.

作者信息

Wallace R A, Hoch K L, Carnevali O

机构信息

Whitney Laboratory, University of Florida, St Augustine 32086.

出版信息

J Mol Biol. 1990 Jun 5;213(3):407-9. doi: 10.1016/S0022-2836(05)80203-7.

DOI:10.1016/S0022-2836(05)80203-7

PMID:2352275

Abstract

N-terminal amino acid sequence data for the small lipovitellin subunits in Xenopus laevis crystalline yolk platelets indicate that LV2 beta is derived from vitellogenin A2 and that LV2 tau is most likely derived from vitellogenin A1. The small lipovitellin subunits apparently commence within the exon 24 region of the parental vitellogenins, flanking the C-terminal end of phosvitin. As a consequence, we conclude that most of the vitellogenin sequence encoded by exons 30 to 35 is not accounted for by the known yolk proteins.

摘要

非洲爪蟾晶状卵黄小板中小脂磷蛋白亚基的N端氨基酸序列数据表明，LV2β源自卵黄生成素A2，LV2τ极有可能源自卵黄生成素A1。小脂磷蛋白亚基显然起始于亲本卵黄生成素的外显子24区域，位于卵黄高磷蛋白C端末端的两侧。因此，我们推断外显子30至35编码的大部分卵黄生成素序列并不包含在已知的卵黄蛋白中。