Staros J V
Biochemistry. 1982 Aug 17;21(17):3950-5. doi: 10.1021/bi00260a008.
We have synthesized and characterized N-hydroxysulfosuccinimide, a new hydrophilic ligand for the preparation of active esters. We have incorporated this ligand into two new protein cross-linking reagents, 3,3'-dithiobis(sulfosuccinimidyl propionate) and bis(sulfosuccinimidyl) suberate. In experiments with rabbit muscle aldolase, it is demonstrated that both of these reagents are highly efficient protein cross-linkers at physiological pH and that 3,3'-dithiobis(sulfosuccinimidyl propionate) is quantitatively cleavable by reduction under mild conditions. In experiments with intact human erythrocytes and erythrocyte membranes, it is shown that both reagents are membrane impermeant and that when erythrocytes are treated with either reagent, both cross-link subunits of the anion channel (band 3) to covalent dimers at the extracytoplasmic membrane face.
我们合成并表征了N-羟基磺基琥珀酰亚胺,一种用于制备活性酯的新型亲水性配体。我们已将此配体并入两种新型蛋白质交联试剂,3,3'-二硫代双(磺基琥珀酰亚胺基丙酸酯)和双(磺基琥珀酰亚胺基)辛二酸酯。在兔肌肉醛缩酶实验中,证明这两种试剂在生理pH下都是高效的蛋白质交联剂,并且3,3'-二硫代双(磺基琥珀酰亚胺基丙酸酯)在温和条件下可通过还原定量裂解。在完整的人红细胞和红细胞膜实验中,表明这两种试剂都不能透过膜,并且当用任何一种试剂处理红细胞时,两种试剂都会使阴离子通道(带3)的亚基在细胞外膜表面交联成共价二聚体。