Ryall R L, Goldrick R B
Lipids. 1977 Mar;12(3):272-7. doi: 10.1007/BF02533346.
The presence of glycerokinase has been demonstrated in human omental and subcutaneous adipose tissue. The enzyme reaction showed a linear time course for 5 min at 30 C and pH optima at pH 7.6 and 9.0. Saturation of the enzyme was observed at 1.8 mM adenosine triphosphate (ATP) and the double reciprocal plot of activity vs. ATP concentration was nonlinear giving two apparent Km values of 0.094 and 0.518 mM. The apparent Km for glycerol, 0.112 mM, was obtained from a linear double reciprocal plot, and the enzyme was saturated at about 0.4 mM glycerol. The activity of glycerokinase in human adipose tissue excised under general anaesthesia was low and was unrelated to adipose cell size or the degree of obesity of the subject from whom the fat was obtained.
已在人体网膜和皮下脂肪组织中证实存在甘油激酶。该酶反应在30℃下5分钟呈线性时间进程，最适pH值为7.6和9.0。在1.8 mM三磷酸腺苷（ATP）时观察到酶的饱和，活性与ATP浓度的双倒数图呈非线性，给出两个表观Km值，分别为0.094和0.518 mM。甘油的表观Km值为0.112 mM，由线性双倒数图得出，该酶在约0.4 mM甘油时饱和。全身麻醉下切除的人体脂肪组织中甘油激酶的活性较低，且与脂肪细胞大小或获取脂肪的受试者的肥胖程度无关。
