Wooten M W, Nel A E, Goldschmidt-Clermont P J, Galbraith R M, Wrenn R W
FEBS Lett. 1985 Oct 21;191(1):97-101. doi: 10.1016/0014-5793(85)81001-2.
A major 56 kDa substrate for phospholipid/Ca2+-dependent kinase (C-kinase) in pancreatic acinar cells is physicochemically and immunologically indistinguishable from the vitamin D-binding protein, Gc or group-specific component. Cellular Gc was also phosphorylated in intact cells following treatment with carbachol as a physiological stimulus. These findings indicate the potential usefulness of Gc as a defined substrate for further studies of the biological role of C-kinase activity in pancreatic acini and possibly in other cells.
胰腺腺泡细胞中磷脂/钙离子依赖性激酶（C激酶）的一种主要56 kDa底物在物理化学性质和免疫学上与维生素D结合蛋白、Gc或组特异性成分无法区分。在用卡巴胆碱作为生理刺激处理完整细胞后，细胞中的Gc也会发生磷酸化。这些发现表明，Gc作为一种明确的底物，对于进一步研究C激酶活性在胰腺腺泡以及可能在其他细胞中的生物学作用具有潜在的用途。
