Silva F J, Bel Y, Botella L M, Cotton R G, Ferré J
Departament de Genètica, Universitat de València, Burjassot, Spain.
Biochem J. 1992 Oct 1;287 ( Pt 1)(Pt 1):85-9. doi: 10.1042/bj2870085.
A monoclonal antibody raised against monkey liver phenylalanine hydroxylase (PAH) has been used to detect this protein in Drosophila melanogaster. A cross-reacting material (CRM) band of apparent molecular mass 50-52 kDa, equivalent to that deduced for the Drosophila melanogaster PAH protein based on the pah gene cDNA sequence, has been detected. This CRM was analysed throughout development and showed an equivalent pattern to that reported for PAH activity in this insect, with maxima at pupariation and at pharate adult formation. Distribution of this CRM in larval tissues, the haemolymph and the adult body is mainly restricted to the larval fat body and the adult head. Demonstration of this CRM as the PAH protein comes from the correlation between the decreased PAH enzyme activities of two mutant strains and their decreased amounts of CRM by Western blotting.
一种针对猴肝苯丙氨酸羟化酶（PAH）产生的单克隆抗体已被用于检测黑腹果蝇中的这种蛋白质。已检测到一条表观分子量为50 - 52 kDa的交叉反应物质（CRM）条带，这与基于pah基因cDNA序列推导的黑腹果蝇PAH蛋白分子量相当。对该CRM在整个发育过程中进行了分析，其模式与报道的这种昆虫中PAH活性模式相同，在化蛹期和成虫形成期达到最大值。该CRM在幼虫组织、血淋巴和成虫体内的分布主要局限于幼虫脂肪体和成虫头部。通过蛋白质免疫印迹法证明该CRM就是PAH蛋白，这源于两个突变菌株的PAH酶活性降低与其CRM含量减少之间的相关性。
