Postgraduate School of Studies in Biological Sciences, University of Bradford, Bradford, Yorkshire BD7 1DP, England.
Plant Physiol. 1976 Dec;58(6):773-6. doi: 10.1104/pp.58.6.773.
Ribulose 1,5-diphosphate carboxylase was isolated from Euglena gracilis Klebs strain Z Pringsheim, Chlorella fusca var. vacuolata, and Chlamydobotrys stellata, and the subunits from each enzyme were separated and purified by gel filtration on Sephadex G-200 in the presence of sodium dodecyl sulfate. Rabbit antibody was elicited against purified Euglena ribulose 1,5-diphosphate carboxylase whole enzyme and the isolated large and small subunits. Euglena ribulose 1,5-diphosphate carboxylase showed partial immunological identity on Ouchterlony gels with the Chlorella and Chlamydobotrys carboxylases. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of immunoprecipitates between antibody to the Euglena large subunit and the isolated large subunits of the Chlorella and Chlamydobotrys enzymes showed this was due to determinants on the large subunit. There was no serological affinity between the small subunits of the Euglena, Chlorella, and Chlamydobotrys carboxylases, and NH(2)-terminal amino acid analyses provided further evidence of variability in the structure of the small subunits.
核酮糖 1,5-二磷酸羧化酶从眼虫 Euglena gracilis Klebs 株 Z Pringsheim、绿球藻 Chlorella fusca var. vacuolata 和星杆藻 Chlamydobotrys stellata 中分离出来，每种酶的亚基都通过在十二烷基硫酸钠存在下在 Sephadex G-200 上进行凝胶过滤来分离和纯化。针对纯化的眼虫核酮糖 1,5-二磷酸羧化酶全酶和分离的大亚基和小亚基，用兔抗体进行了免疫。在 Ouchterlony 凝胶上，眼虫核酮糖 1,5-二磷酸羧化酶与绿球藻和星杆藻羧化酶表现出部分免疫学同一性。用针对 Euglena 大亚基的抗体与 Chlorella 和 Chlamydobotrys 酶的分离大亚基进行免疫沉淀的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析表明，这是由于大亚基上的决定簇所致。Euglena、Chlorella 和 Chlamydobotrys 羧化酶的小亚基之间没有血清亲和力，并且 NH2-末端氨基酸分析进一步提供了小亚基结构变异性的证据。
