Lebeche D, Lucero H A, Kaminer B
Department of Physiology, Boston University School of Medicine, MA 02118.
Biochem Biophys Res Commun. 1994 Jul 15;202(1):556-61. doi: 10.1006/bbrc.1994.1964.
We have characterized the Ca2+ binding properties of protein disulfide isomerase (PDI). It binds 19 mol Ca2+/mol protein with low affinity, which is reduced by increasing the ionic strength. Ca2+ induced conformational changes detected by UV difference spectroscopy. These Ca2+ binding properties resemble those of a sea urchin egg 58 kDa protein.
我们已经对蛋白质二硫键异构酶（PDI）的钙离子结合特性进行了表征。它以低亲和力结合19摩尔钙离子/摩尔蛋白质，这种亲和力会随着离子强度的增加而降低。通过紫外差光谱检测到钙离子诱导的构象变化。这些钙离子结合特性类似于海胆卵58 kDa蛋白的特性。
