Margolis F L, Grillo M, Brown C E, Williams T H, Pitcher R G, Elgar G J
Biochim Biophys Acta. 1979 Oct 11;570(2):311-23. doi: 10.1016/0005-2744(79)90151-7.
Carnosinase (aminoacyl-L-histidine hydrolase, EC 3.4.13.3) hydrolyzes the dipeptide carnosine (beta-alanyl-L-histidine), which is thought to play a role in cerebral and skeletal muscular function and has been implicated as a neuroaffector in the olfactory bulb. Carnosinase activity is present in many tissues of the mouse including heart, liver and lung, but it is most active in kidney, uterus and nasal olfactory mucosa. Kinetic measurements with 1H-NMR spectroscopy indicate that the enzyme is stereospecific and can hydrolyze L-but not D-carnosine. Anserine is a poorer substrate, while homocarnosine is essentially a non-substrate. However, these two dipeptides are effective inhibitors of the hydrolysis of L-carnosine. Carnosinase activity is unaffected when assayed in 2H2O at 99% isotopic purity. From considerations of the effect of Mn2+ on (1) substrate concentration velocity curves; (2) thermostability, and (3) inhibitor behavior, tissues with carnosinase can be divided into two groups. Kidney, uterus and olfactory mucosa represent one group, while central nervous system, muscle, spleen, etc. represent the second. The validity of this classification is confirmed by immunological evidence. Antiserum prepared against carnosinase purified from kidney cross-reacts with and inhibits the activity of olfactory mucosa, kidney and uterus but not that from central nervous system, heart or liver.
肌肽酶（氨基酰-L-组氨酸水解酶，EC 3.4.13.3）可水解二肽肌肽（β-丙氨酰-L-组氨酸），肌肽被认为在大脑和骨骼肌功能中发挥作用，并且在嗅球中被认为是一种神经影响因子。肌肽酶活性存在于小鼠的许多组织中，包括心脏、肝脏和肺，但在肾脏、子宫和鼻嗅黏膜中活性最高。用1H-NMR光谱进行动力学测量表明，该酶具有立体特异性，能够水解L-肌肽而不能水解D-肌肽。鹅肌肽是较差的底物，而高肌肽基本上是非底物。然而，这两种二肽是L-肌肽水解的有效抑制剂。当在同位素纯度为99%的2H2O中进行测定时，肌肽酶活性不受影响。从Mn2+对（1）底物浓度-速度曲线；（2）热稳定性和（3）抑制剂行为的影响考虑，含有肌肽酶的组织可分为两组。肾脏、子宫和嗅黏膜代表一组，而中枢神经系统、肌肉、脾脏等代表另一组。这种分类的有效性通过免疫学证据得到证实。针对从肾脏纯化的肌肽酶制备的抗血清与嗅黏膜、肾脏和子宫的肌肽酶发生交叉反应并抑制其活性，但不与中枢神经系统、心脏或肝脏的肌肽酶发生交叉反应。
