Coates P M, Cortner J A, Hoffman G M, Brown S A
Biochim Biophys Acta. 1979 Feb 26;572(2):225-34. doi: 10.1016/0005-2760(79)90038-9.
Acid lipase activity was examined in human leukocytes using 4-methylumbelliferyl esters in a fluorimetric assay. Mononuclear leukocytes had 10--15 times the acid lipase activity of polymorphonuclear leukocytes. The enzyme activity was highest using the oleate ester of 4-methylumbelliferone at pH 4.0, in the presence of L-alpha-phosphatidylcholine and taurodeoxycholic acid (sodium salt). Acid lipase activity was inhibited by diethylaminoethoxyhexestrol, sodium chloride and fluoride, potassium chloride, calcium chloride and albumin, but was unaffected by diethyl p-nitrophenyl phosphate or sulphydryl reagents. There were at least two forms of acid lipase activity: one (A form) was sensitive to heart inactivation (56 degrees C) and corresponded to the enzyme deficient in patients with Wolman's disease; the other (B form) was resistant to heat inactivation and corresponded to the residual enzyme activity found in Wolman's disease.
采用荧光分析法，使用4-甲基伞形酮酯检测人白细胞中的酸性脂肪酶活性。单核白细胞的酸性脂肪酶活性是多形核白细胞的10至15倍。在pH 4.0条件下，于L-α-磷脂酰胆碱和牛磺脱氧胆酸钠存在时，使用4-甲基伞形酮的油酸酯时酶活性最高。酸性脂肪酶活性受到二乙氨基乙氧基己烯雌酚、氯化钠和氟化物、氯化钾、氯化钙和白蛋白的抑制，但不受对硝基苯基磷酸二乙酯或巯基试剂的影响。酸性脂肪酶活性至少有两种形式：一种（A形式）对热灭活（56℃）敏感，相当于沃曼病患者中缺乏的酶；另一种（B形式）对热灭活有抗性，相当于沃曼病中发现的残余酶活性。
