Berne C
Enzyme. 1976;21(2):127-36. doi: 10.1159/000458851.
A sensitive assay for d-3hydroxybutrate dehydrogenase (EC 1.1.1.30) was developed for use with the minute amounts of material obtained from islets of Langerhans microdissected from freeze-dried pancreatic sections. NADH formed in the enzyme reaction was determined by photokinetic analysis of the luminescence obtained with bacterial luciferase from Achromobacter fishcherii. In this way, accurate determination was obtained with less than 0.1 mug dry weight of islet material. In obese hyperglycemic mice, the islet enzyme had an activity of 4.7 mumoles/min and g dry weight. Optimal enzyme activity was found at pH 8 for the islet enzyme. The enzyme activity was similar in pancreatic islets and acini, while considerably higher activity was found in cardiac muscle, liver and renal cortex. Normal mouse islets showed about equal enzyme activity as the islets from obese hyperglycemic mice.
已开发出一种用于检测d-3-羟基丁酸脱氢酶（EC 1.1.1.30）的灵敏测定法，用于检测从冻干胰腺切片中显微切割得到的胰岛所获取的微量物质。酶反应中形成的NADH通过对来自费氏无色杆菌的细菌荧光素酶产生的发光进行光动力学分析来测定。通过这种方法，使用少于0.1微克干重的胰岛物质即可获得准确测定结果。在肥胖高血糖小鼠中，胰岛酶的活性为4.7微摩尔/分钟·克干重。该胰岛酶在pH 8时具有最佳酶活性。胰腺胰岛和腺泡中的酶活性相似，而在心肌、肝脏和肾皮质中发现的酶活性则高得多。正常小鼠胰岛的酶活性与肥胖高血糖小鼠的胰岛酶活性大致相当。
