钙／钙调素依赖性蛋白激酶对17．7kD和6kD胰腺蛋白的磷酸化  

The Phosphorylation of 17.7 kD and 6 kD Pancreatic Proteins by Ca￣(2+)/CaM-dependent Protein Kinase

作　　者：李翠凤[1] 凌启阆[1] 王军[1] 尚克进[1] 

机构地区：[1]南开大学生物系生化教研室

出　　处：《生物化学杂志》1994年第2期185-190,共6页

基　　金：国家自然科学基金

摘　　要：本文报导了胰腺提取物中两种可被钙／钙调素依赖性蛋白激酶磷酸化的热稳定蛋白。ＳＤＳ－ＰＡＧＥ测定其表观分子量分别为１７．７ｋＤ和６ｋＤ。经钙／钙调素依赖性蛋白激酶磷酸化后，其最大磷酸参入量为８．８μｍｏｌ／ｇ蛋白。同时磷酸化作用导致１７．７ｋＤ蛋白在ＳＤＳ－ＰＡＧＥ中迁移率发生变化。本文还进一步分析了各种阳离子对磷酸化的影响，并对此两种蛋白可能具有的生理功能进行了初步探讨。In the present study, two kinds of heat stable proteins extracted from porcine pancreas were reported. The proteins can be phosphorylated by Ca￣(2+)/CaM-dependent protein kinase and the maximal phosphate incorporation is 8.8 μmol/g protein. The apparent rnolecular weights (Wr) of the two proteins are 17.7 kD and 6 kD in SDS-polyacrylamide gels respectively. Phosphorylation of 17.7 kD protein induced mobility shift in SDS-gel, unphosphorylated protein migrated with an apparent Mr 17.7kD, phosphorylation of the protein decreased the apparent Mr to 17 kD. We have also shown the effects of some cations on phosphorylation of pancreatic proteins. The possible physiological functions of these proteins were discussed.

关 键 词：胰腺 蛋白 磷酸化 钙 调钙蛋白 

分 类 号：Q593.9[生物学—生物化学]