人类胰液中是否存在特定的溶血磷脂酶？

Is there a specific lysophospholipase in human pancreatic juice?

作者信息

Duan R D, Borgström B

机构信息

Department of Medical and Physiological Chemistry, University of Lund, Sweden.

出版信息

Biochim Biophys Acta. 1993 Apr 23;1167(3):326-30. doi: 10.1016/0005-2760(93)90236-3.

DOI:10.1016/0005-2760(93)90236-3

PMID:8481395

Abstract

The existence of a specific lysophospholipase in human pancreatic juice was evaluated. The proteins were separated by a series of chromatographic steps including Sephacryl S-200, cholate-Sepharose 4B, Sephadex G-100 and CM-Sephadex G-50. The enzyme activities against 1-palmitoyl lysolecithin (LL) as well as tributyrin (TB) and p-nitrophenyl butyrate (PNPB) were determined in all the fractions of these purification procedures. Enzyme activity against LL was always eluted in parallel with activities against TB and PNPB, and no unique activity against LL could be found. The specific activity against LL was 40-times lower than that against PNPB and 200-times lower than that against TB. It is concluded that there is no unique lysophospholipase in human pancreatic juice and that the hydrolysis of lysolecithin is most likely performed by carboxyl ester lipase.

摘要

对人胰液中特异性溶血磷脂酶的存在情况进行了评估。蛋白质通过一系列色谱步骤进行分离，包括Sephacryl S - 200、胆酸盐 - Sepharose 4B、Sephadex G - 100和CM - Sephadex G - 50。在这些纯化步骤的所有级分中，测定了针对1 - 棕榈酰溶血卵磷脂（LL）以及三丁酸甘油酯（TB）和对硝基苯丁酸酯（PNPB）的酶活性。针对LL的酶活性总是与针对TB和PNPB的活性平行洗脱，未发现针对LL的独特活性。针对LL的比活性比对PNPB的低40倍，比对TB的低200倍。得出的结论是，人胰液中不存在独特的溶血磷脂酶，溶血卵磷脂的水解很可能是由羧基酯脂肪酶进行的。