Maier M, Reissert G, Jerabek I, Lottspeich F, Binder B R
Department of Medical Physiology, University of Vienna, Austria.
FEBS Lett. 1988 May 23;232(2):395-8. doi: 10.1016/0014-5793(88)80778-6.
The types of kinins released from purified native, single chain human high and low molecular mass kininogens (HMMKs and LMMKs, respectively) by purified human urinary kallikrein were separated by reverse-phase HPLC and quantitated by the rat uterus bioassay. [Hyp3]-lysyl-bradykinin, a recently discovered kinin, represented up to 58% of the biological activity released from 4 individual HMMK preparations purified from 4 different healthy volunteers. In contrast, the majority of the biological activity released from LMMKs purified from pooled plasma was identified as Lys-bradykinin and [Hyp3]-lysyl-bradykinin represented only 6.4 +/- 3.8%. These findings indicate posttranslation hydroxylation of human kininogens and suggest a preference of HMMKs for this modification.
通过纯化的人尿激肽释放酶从纯化的天然单链人高分子量和低分子量激肽原(分别为HMMKs和LMMKs)中释放的激肽类型,通过反相高效液相色谱法分离,并通过大鼠子宫生物测定法定量。[Hyp3]-赖氨酰缓激肽是最近发现的一种激肽,在从4名不同健康志愿者纯化的4种单独HMMK制剂中释放的生物活性中占比高达58%。相比之下,从混合血浆中纯化的LMMKs释放的大部分生物活性被鉴定为赖氨酰缓激肽,而[Hyp3]-赖氨酰缓激肽仅占6.4±3.8%。这些发现表明人激肽原存在翻译后羟基化,并提示HMMKs对这种修饰有偏好。