Gettins P G, Beechem J M, Crews B C
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146.
FEBS Lett. 1993 Jul 5;325(3):267-70. doi: 10.1016/0014-5793(93)81086-f.
To determine whether integrity of the bait region affects the structure of the remainder of human alpha 2-macroglobulin (alpha 2M), we have determined the separation between cysteine residues in a methylamine-reacted fast-form of alpha 2M. From reduction in fluorescence intensity of covalently-bound donor fluorophore caused by proximity to an acceptor, a separation of 35 +/- 8 A was calculated, which is identical to a previously determined value for proteinase-treated fast-form alpha 2M. This indicates that although bait region cleavage is the physiological route to conformational change in alpha 2M, bait region integrity per se does not significantly affect the structure of fast-form alpha 2M.
为了确定诱饵区域的完整性是否会影响人α2-巨球蛋白(α2M)其余部分的结构,我们测定了甲胺反应的快速形式α2M中半胱氨酸残基之间的间距。通过靠近受体导致的共价结合供体荧光团荧光强度的降低,计算出间距为35±8埃,这与先前测定的蛋白酶处理的快速形式α2M的值相同。这表明,虽然诱饵区域的切割是α2M构象变化的生理途径,但诱饵区域的完整性本身并不会显著影响快速形式α2M的结构。