Honda T, Hitomi Y, Niinobe M, Fujii S
Histochemistry. 1983;77(3):299-302. doi: 10.1007/BF00490892.
The proteases of human leukocytes were cytochemically studied by use of new alpha-naphthyl esters, tosyl-L-lysine-alpha-naphthyl ester (TLNE) and acetyl-L-tyrosine-alpha-naphthyl ester (ATNE). The hydrolytic activities were strong only in neutrophils, with both substrates. They were inhibited completely by DFP and chymostatin, but not by leupeptin and iodoacetate. These results indicate that chymotrypsin-like enzyme(s), capable of hydrolyzing both substrates, exist in neutrophils.
利用新型α-萘酯、甲苯磺酰-L-赖氨酸-α-萘酯（TLNE）和乙酰-L-酪氨酸-α-萘酯（ATNE），对人白细胞蛋白酶进行了细胞化学研究。两种底物在中性粒细胞中的水解活性均很强。它们完全被二异丙基氟磷酸（DFP）和抑糜酶素抑制，但不被亮抑酶肽和碘乙酸抑制。这些结果表明，中性粒细胞中存在能够水解两种底物的类胰凝乳蛋白酶。
