Nitsos R E, Evans H J
Plant Physiol. 1966 Nov;41(9):1499-504. doi: 10.1104/pp.41.9.1499.
An investigation has been made to determine the effectiveness of univalent cations as cofactors for the inductive synthesis of nitrate reductase. In these experiments K(+) functions more effectively as the univalent cation activator than other univalent cations. Substitution of Rb(+) for K(+) resulted in enzyme formation at a rate of about one-half of that obtained with K(+). Sodium, Li(+), or NH(4) (+) either failed to stimulate or completely inhibited the inductive formation of the enzyme. When no univalent cations were present in the induction medium, enzyme formation was delayed for an initial 3-hour period in contrast to the normal one-hour delay in enzyme formation where adequate K(+) was present in the induction medium. During the period of inductive formation of nitrate reductase the activity of pyruvic kinase, a constitutive enzyme, was assayed under conditions where adequate K(+) was present. Results indicate that the presence of the different univalent cations in the induction medium had no striking effect on the activity of this enzyme during the induction period.
已开展一项研究以确定单价阳离子作为硝酸盐还原酶诱导合成辅因子的有效性。在这些实验中,K(+)作为单价阳离子激活剂比其他单价阳离子更有效。用Rb(+)替代K(+)导致酶形成的速率约为用K(+)时的一半。钠、Li(+)或NH(4) (+)要么未能刺激要么完全抑制该酶的诱导形成。当诱导培养基中不存在单价阳离子时,与诱导培养基中存在足够K(+)时酶形成正常延迟一小时相比,酶形成最初延迟3小时。在硝酸盐还原酶诱导形成期间,在存在足够K(+)的条件下测定组成型酶丙酮酸激酶的活性。结果表明,诱导培养基中不同单价阳离子的存在在诱导期对该酶的活性没有显著影响。