Bousset-Risso M, Bonicel J, Rovery M
FEBS Lett. 1985 Mar 25;182(2):323-6. doi: 10.1016/0014-5793(85)80325-2.
Mild chymotrypsin digestion of native lipase (449 amino acids) preferentially cleaved the Phe 335-Ala 336 bond. On SDS-gel electrophoresis, 3 major bands were observed: band 1 (52 kDa) representing native lipase, bands 2 and 3 (40 and 12 kDa) representing the two lipase fragments A and B. Fragment A does not retain lipase activity but maintains its ability to adsorb to interfaces. Fragment B was identified with the lipase C-terminal region (336-449). It does not exhibit any activity towards tributyrylglycerol emulsions and any ability to adsorb to interfaces.
用温和的胰凝乳蛋白酶消化天然脂肪酶（449个氨基酸）时，优先切割苯丙氨酸335-丙氨酸336键。在SDS凝胶电泳上观察到3条主要条带：条带1（52 kDa）代表天然脂肪酶，条带2和条带3（40和12 kDa）代表脂肪酶的两个片段A和B。片段A不保留脂肪酶活性，但保持其吸附到界面的能力。片段B被鉴定为脂肪酶的C末端区域（336-449）。它对三丁酰甘油乳液没有任何活性，也没有吸附到界面的能力。
