DeNigris S J, Hamosh M, Kasbekar D K, Lee T C, Hamosh P
Department of Physiology and Biophysics, Georgetown University Medical Center, Washington, DC 20007.
Biochim Biophys Acta. 1988 Mar 4;959(1):38-45. doi: 10.1016/0005-2760(88)90147-6.
The source of the lipase(s) acting in the stomach was investigated in five animal species: rat, mouse (rodents), rabbit (lagomorphs), guinea pig (caviidae), baboon and human (primates). The activity of lingual and gastric lipases was quantitated in homogenates of lingual serous glands and of gastric mucosa, respectively, by the hydrolysis of tri[3H]oleylglycerol and is expressed in units/g (1 U = 1 mumol [3H]oleic acid released/min) per g tissue wet weight, mean +/- S.E. There were marked differences in the activity level of lingual and gastric lipases among species: mouse and rat had high levels of lingual lipase activity (250 +/- 20 and 824 +/- 224 U/g) and only traces of gastric lipase activity (4.5 +/- 0.9 and 0.04 U/g, respectively), whereas rabbit and guinea pig had no lingual lipase activity and only gastric lipase activity (78 +/- 48 and 27 +/- 7.4 U/g, respectively). In the baboon and human, gastric lipase was the predominant enzyme (109 +/- 20 U/g and 118 +/- 8.8 U/g, respectively), whereas lingual lipase activity was present in trace amounts only (0.04 U/g and 0.3 U/g, respectively). In addition to species differences in the origin of the preduodenal lipases, there were also species differences in the distribution of gastric lipase in the stomach. Thus, while in the rabbit, gastric lipase was localized exclusively in the cardia and body of the stomach, it was diffusely distributed in the entire stomach of the guinea pig and baboon. A comparison between the level of activity of lipase and pepsin (the two chief digestive enzymes secreted by the stomach), showed differences in their localization in the species studied. The difference in source (tongue vs. stomach) and site (cardia-body vs. entire stomach) of lipase secretion must be taken into account in future studies of these digestive enzymes. Although the exact contribution of lingual and gastric lipases individually to fat digestion in species which contain both enzymes cannot yet be evaluated, the markedly higher levels of gastric lipase activity in the baboon and human suggests that, in primates, gastric lipase is probably the major non-pancreatic digestive lipase.
大鼠、小鼠（啮齿动物）、兔子（兔形目动物）、豚鼠（豚鼠科动物）、狒狒和人类（灵长类动物）。分别通过三[³H]油酰甘油的水解来定量舌浆液腺和胃黏膜匀浆中舌脂肪酶和胃脂肪酶的活性，并以单位/克（1 U =每分钟释放1 μmol [³H]油酸）表示，以每克组织湿重计，均值±标准误。不同物种之间舌脂肪酶和胃脂肪酶的活性水平存在显著差异：小鼠和大鼠的舌脂肪酶活性水平较高（分别为250±20和824±224 U/g），而胃脂肪酶活性仅为微量（分别为4.5±0.9和0.04 U/g），而兔子和豚鼠没有舌脂肪酶活性，只有胃脂肪酶活性（分别为78±48和27±7.4 U/g）。在狒狒和人类中，胃脂肪酶是主要的酶（分别为109±20 U/g和118±8.8 U/g），而舌脂肪酶活性仅为微量（分别为0.04 U/g和0.3 U/g）。除了十二指肠前脂肪酶来源的物种差异外，胃脂肪酶在胃中的分布也存在物种差异。因此，在兔子中，胃脂肪酶仅定位在胃的贲门和体部，而在豚鼠和狒狒的整个胃中呈弥散分布。对脂肪酶和胃蛋白酶（胃分泌的两种主要消化酶）活性水平的比较显示，在所研究的物种中它们的定位存在差异。在未来对这些消化酶的研究中，必须考虑脂肪酶分泌来源（舌与胃）和部位（贲门 - 体部与整个胃）的差异。尽管在同时含有这两种酶的物种中，舌脂肪酶和胃脂肪酶各自对脂肪消化的确切贡献尚无法评估，但狒狒和人类中胃脂肪酶活性明显较高表明，在灵长类动物中，胃脂肪酶可能是主要的非胰腺消化脂肪酶。
