Ratner S
Proc Natl Acad Sci U S A. 1982 Sep;79(17):5197-9. doi: 10.1073/pnas.79.17.5197.
Homogeneous crystalline argininosuccinate synthetase [L-citrulline:L-aspartate ligase (AMP-forming), EC 6.3.4.5] prepared from bovine liver according to Rochovansky et al. [Rochovansky, O., Kodowaki, H. & Ratner, S. (1977)J. Biol. Chem. 252, 5287-5294] has been characterized with respect to amino acid composition and other chemical and physical properties. The total residue molecular weights derived from the amino acid analysis are in agreement with values previously obtained by physical means for the catalytically active tetramer, 185,000, and the monomer, 46,500. The enzyme is focused sharply at pH 7.6 as a single protein. Additional properties reported include 2.74 X 10(5) M-1 cm-1 for the molar absorption coefficient, based on the absolute value for protein, and 0.747 ml/g for the chemically based partial specific volume.
按照罗乔万斯基等人[罗乔万斯基,O.,小户和木,H.与拉特纳,S.(1977年)《生物化学杂志》252卷,5287 - 5294页]所述方法从牛肝脏中制备的均一结晶精氨琥珀酸合成酶[L - 瓜氨酸:L - 天冬氨酸连接酶(生成AMP),EC 6.3.4.5],已就其氨基酸组成以及其他化学和物理性质进行了表征。由氨基酸分析得出的总残基分子量与先前通过物理方法得到的催化活性四聚体(185,000)和单体(46,500)的值一致。该酶作为单一蛋白质在pH 7.6处聚焦明显。报道的其他性质包括基于蛋白质绝对值的摩尔吸收系数为2.74×10⁵ M⁻¹ cm⁻¹,以及基于化学方法的比容为0.747 ml/g。