Maruniak J E, Summers M D, Falcon L A, Smith G E
Intervirology. 1979;11(2):82-8. doi: 10.1159/000149017.
Polyhedrin obtained from Autographa californica nuclear polyhedrosis virus (AcMNPV) was apparently not modified in terms of primary structure after passage through alternate host systems, both in vivo and in vitro, as investigated by two-dimensional, high-voltage electrophoresis of tryptic digests of this protein as well as amino acid analysis. N-terminal analyses were conducted using an improved technique which showed proline to be the N-terminal amino acid. In addition, passage of enveloped nucleocapsids through alternate hosts as studied by SDS-PAGE showed the polypeptide compositions to be very similar.
通过对该蛋白胰蛋白酶消化产物进行二维高压电泳以及氨基酸分析发现，从苜蓿银纹夜蛾核型多角体病毒（AcMNPV）中获得的多角体蛋白，在体内和体外经过交替宿主系统传代后，其一级结构显然未发生改变。使用一种改进技术进行了N端分析，结果表明脯氨酸是N端氨基酸。此外，通过SDS-PAGE研究包膜核衣壳在交替宿主中的传代情况，结果显示多肽组成非常相似。
