D'Souza T M, Oriel P
Department of Microbiology and Public Health, Michigan State University, East Lansing 48824-1101.
Appl Biochem Biotechnol. 1992 Sep;36(3):183-98. doi: 10.1007/BF02921778.
Lamb pregastric lipase was purified from a commercial source using delipidation, solubilization with KSCN, acid-precipitation, pepsin-digestion, affinity chromatography with agarose-Cibacron Blue F3GA, gel filtration, and elution from a native 10% (w/v) polyacrylamide gel. The enzyme had a single subunit of 68,000 Da with maximum esterase activity when measured at pH 6.0 and 30 degrees C. The enzyme preferentially hydrolyzed short- and medium-chain (C4, C6, and C8) synthetic esters and short-chain (C4 and C6) monoacid triglycerides. The NH2-terminal sequence demonstrated high homology with gastric and lingual lipases.
羔羊前胃脂肪酶是从商业来源纯化得到的，采用了脱脂、用硫氰酸钾增溶、酸沉淀、胃蛋白酶消化、用琼脂糖-汽巴蓝F3GA进行亲和层析、凝胶过滤以及从天然10%（w/v）聚丙烯酰胺凝胶上洗脱等方法。该酶具有一个68,000 Da的单亚基，在pH 6.0和30℃测定时具有最大酯酶活性。该酶优先水解短链和中链（C4、C6和C8）合成酯以及短链（C4和C6）单酸甘油酯。其氨基末端序列与胃脂肪酶和舌脂肪酶具有高度同源性。
