Lake B D, Ellis R B
Histochem J. 1976 Jul;8(4):357-66. doi: 10.1007/BF01003824.
The effect of a standard method of fixation (formalin-calcium 24 hr at 4 degrees C, followed by washing in gum-sucrose) on the activity of three lysosomal enzymes (N-acetyl-beta-D-glucosaminidase, acid phosphatase, beta-D-galactosidase) in the liver of three species (human, rabbit, lamb) was studied by biochemical methods, and the results were compared with staining intensities in histochemical preparations of the same tissues. The following conclusions were reached: (1) Fixation by formaldehyde changes the characteristics of the enzymes and makes comparisons between biochemistry and histochemistry difficult to interpret; (2) The intensity of staining in fixed or unfixed tissue sections bears no relation to absolute levels of enzyme activity; (3) Changes in staining intensity of a particular enzyme activity in a particular organ of a particular species prepared in a particular way are significant. Quantifying these changes is useful, as long as absolute values are not considered, and it is realized that it is only the difference that is being quantified.
采用生化方法研究了一种标准固定方法（4℃下用甲醛 - 钙固定24小时，随后在树胶 - 蔗糖中洗涤）对三种物种（人类、兔子、羔羊）肝脏中三种溶酶体酶（N - 乙酰 - β - D - 氨基葡萄糖苷酶、酸性磷酸酶、β - D - 半乳糖苷酶）活性的影响，并将结果与相同组织的组织化学制剂中的染色强度进行了比较。得出以下结论：（1）甲醛固定会改变酶的特性，使得生物化学和组织化学之间的比较难以解释；（2）固定或未固定组织切片中的染色强度与酶活性的绝对水平无关；（3）以特定方式制备的特定物种特定器官中特定酶活性的染色强度变化具有显著性。只要不考虑绝对值，并认识到所量化的只是差异，对这些变化进行量化是有用的。
