Kagan H M
Connect Tissue Res. 1978;6(3):167-9. doi: 10.3109/03008207809152627.
The interaction of sodium dodecyl sulfate with elastin has been studied by complexometric titration. Approximately 1.2 mumoles of protons with a pKapp of 5.45 are taken up by 10 milligrams of insoluble elastin upon the binding of detergent, apparently due to the protonation of normally ionized carboxylate functions in this protein. Since ionized carboxylate functions of elastin are essential for its interaction with elastase and, possibly, metallic cations, these results may have physiological significance in view of the affinity of elastin for lipid-like ligands.
通过络合滴定法研究了十二烷基硫酸钠与弹性蛋白的相互作用。在洗涤剂结合后，10毫克不溶性弹性蛋白会吸收约1.2微摩尔pKapp为5.45的质子，这显然是由于该蛋白质中正常离子化的羧酸盐官能团发生了质子化。由于弹性蛋白的离子化羧酸盐官能团对其与弹性蛋白酶以及可能与金属阳离子的相互作用至关重要，鉴于弹性蛋白对类脂配体的亲和力，这些结果可能具有生理学意义。
