Docherty A J, Bodmer M W, Angal S, Verger R, Riviere C, Lowe P A, Lyons A, Emtage J S, Harris T J
Nucleic Acids Res. 1985 Mar 25;13(6):1891-903. doi: 10.1093/nar/13.6.1891.
Purified rat lingual lipase (EC3113), a glycoprotein of approximate molecular weight 52,000, was used to generate polyclonal antibodies which were able to recognise the denatured and deglycosylated enzyme. These immunoglobulins were used to screen a cDNA library prepared from mRNA isolated from the serous glands of rat tongue cloned in E. coli expression vectors. An almost full length cDNA clone was isolated and the nucleotide and predicted amino acid sequence obtained. Comparison with the N-terminal amino acid sequence of the purified enzyme confirmed the identity of the cDNA and indicated that there was a hydrophobic signal sequence of 18 residues. The amino acid sequence of mature rat lingual lipase consists of 377 residues and shares little homology with porcine pancreatic lipase apart from a short region containing a serine residue at an analogous position to the ser 152 of the porcine enzyme.
纯化的大鼠舌脂肪酶（EC3.1.1.3）是一种分子量约为52,000的糖蛋白，被用于制备能够识别变性和去糖基化酶的多克隆抗体。这些免疫球蛋白被用于筛选从大鼠舌浆液性腺分离的mRNA构建的cDNA文库，该文库克隆于大肠杆菌表达载体中。分离出一个几乎全长的cDNA克隆，并获得了核苷酸和预测的氨基酸序列。与纯化酶的N端氨基酸序列比较证实了该cDNA的身份，并表明存在一个18个残基的疏水信号序列。成熟大鼠舌脂肪酶的氨基酸序列由377个残基组成，除了在与猪胰脂肪酶第152位丝氨酸类似位置含有一个丝氨酸残基的短区域外，与猪胰脂肪酶几乎没有同源性。
