Hankins C N, Largen M T, Mills S E
Department of Biology, University of California, San Diego, La Jolla, California 92093.
Plant Physiol. 1976 Jan;57(1):101-4. doi: 10.1104/pp.57.1.101.
Anthranilate synthetase, phosphoribosyltransferase, phosphoribosyl anthranilate isomerase, and indoleglycerol phosphate synthetase were examined in partially purified extracts of the monocotyledon, Zea mays and the dicotyledon, Pisum sativum. The plant extracts were chromatographed on DEAE-cellulose and Sephadex G150. The molecular weights of the enzymes were determined and found to be similar to those observed for many bacteria. None of the plant tryptophan enzyme activities was aggregated in vitro as is also the case with most bacteria. This is in contrast with the complex aggregation patterns observed in other eucaryotic organisms that have been examined (fungi and Euglena gracilis). The tryptophan enzymes from peas and corn were generally similar but some differences in stability were observed.
在单子叶植物玉米和双子叶植物豌豆的部分纯化提取物中,对邻氨基苯甲酸合成酶、磷酸核糖基转移酶、磷酸核糖基邻氨基苯甲酸异构酶和吲哚甘油磷酸合成酶进行了检测。将植物提取物在DEAE - 纤维素和葡聚糖G150上进行色谱分析。测定了这些酶的分子量,发现与许多细菌中观察到的分子量相似。与大多数细菌一样,植物中色氨酸酶的活性在体外均未发生聚集。这与在已检测的其他真核生物(真菌和纤细裸藻)中观察到的复杂聚集模式形成对比。豌豆和玉米中的色氨酸酶总体相似,但在稳定性方面观察到一些差异。