School of Dentistry, Dental Sciences Building-DSB0071, Schulich School of Medicine & Dentistry, The University of Western Ontario, London N6A 5C1, ON, Canada.
J Dent Res. 2011 Feb;90(2):268-72. doi: 10.1177/0022034510388653. Epub 2010 Nov 12.
Histatins are salivary proteins that exhibit a high affinity for hydroxyapatite and contribute to the acquired enamel pellicle. Previous studies have observed that, despite the high proteolytic activity in saliva, significant numbers of histatin molecules in acquired enamel pellicle are intact. Our working hypothesis was that histatins are less susceptible to proteinases present in saliva when adsorbed on the hydroxyapatite. To test this premise, we incubated histatin 1 with hydroxyapatite and human whole saliva. Proteolytic products of this incubation were then characterized by PAGE, HPLC, and mass spectrometry. This study shows for the first time that binding to hydroxyapatite confers intact histatin 1 with resistance to proteolytic degradation.
Histatins 是一种具有高亲和力的唾液蛋白，对获得性牙釉质有贡献。先前的研究观察到，尽管唾液中的蛋白水解活性很高，但获得性牙釉质中的大量组蛋白分子仍然完整。我们的工作假设是，当组蛋白吸附在羟基磷灰石上时，它们对唾液中存在的蛋白酶的敏感性较低。为了验证这一前提，我们将组蛋白 1 与羟基磷灰石和人全唾液孵育。然后通过 PAGE、HPLC 和质谱对孵育的蛋白水解产物进行了表征。这项研究首次表明，与羟基磷灰石结合使完整的组蛋白 1 具有抵抗蛋白水解降解的能力。
