Parker K C, Strominger J L
Biochemistry. 1983 Mar 1;22(5):1145-53. doi: 10.1021/bi00274a024.
Human urinary beta 2-microglobulin (beta 2m) and pa-pain-solubilized human histocompatibility antigen HLA-B7 were iodinated with iodogen and the sites of iodination determined. In the case of free urinary beta 2m, four of the six tyrosines were modified to some degree. Two of these were heavily iodinated (tyrosine-63 and -67) while two were lightly iodinated (tyrosine-10 and -26). In the case of beta 2m iodinated in the intact HLA-B7 complex, only one of these tyrosines was modified substantially (tyrosine-67). beta 2m iodinated at either of the two major sites exchanged into the HLA-B7 complex, whereas beta 2m iodinated at either of the two minor sites did not exchange at all. The relationship of these findings to the quaternary structure of HLA is discussed.
用碘甘氨酸对人尿β2 -微球蛋白（β2m）和木瓜蛋白酶溶解的人组织相容性抗原HLA - B7进行碘化，并确定碘化位点。对于游离的尿β2m，六个酪氨酸中有四个在一定程度上被修饰。其中两个被大量碘化（酪氨酸-63和-67），而另外两个被轻度碘化（酪氨酸-10和-26）。在完整的HLA - B7复合物中碘化的β2m，这些酪氨酸中只有一个被大量修饰（酪氨酸-67）。在两个主要位点之一碘化的β2m可交换到HLA - B7复合物中，而在两个次要位点之一碘化的β2m根本不发生交换。讨论了这些发现与HLA四级结构的关系。
