Dzikowska A, Le Caer J P, Jonczyk P, Wëgleński P
Department of Genetics, Warsaw University, Poland.
Acta Biochim Pol. 1994;41(4):467-71.
Arginase (EC 3.5.3.1) of Aspergillus nidulans, the enzyme which enables the fungus to use arginine as the sole nitrogen source was purified to homogeneity. Molecular mass of the purified arginase subunit is 40 kDa and is similar to that reported for the Neurospora crassa (38.3 kDa) and Saccharomyces cerevisiae (39 kDa) enzymes. The native molecular mass of arginase is 125 kDa. The subunit/native molecular mass ratio suggests a trimeric form of the protein. The arginase protein was cleaved and partially sequenced. Two out of the six polypeptides sequenced show a high degree of homology to conserved domains in arginases from other species.
构巢曲霉的精氨酸酶（EC 3.5.3.1），即一种使该真菌能够将精氨酸作为唯一氮源利用的酶，被纯化至同质。纯化后的精氨酸酶亚基分子量为40 kDa，与报道的粗糙脉孢菌（38.3 kDa）和酿酒酵母（39 kDa）的酶相似。精氨酸酶的天然分子量为125 kDa。亚基/天然分子量比表明该蛋白质为三聚体形式。对精氨酸酶蛋白进行了切割和部分测序。所测序的六条多肽中有两条与其他物种精氨酸酶的保守结构域具有高度同源性。
