Trommer W E, Friebel K, Kiltz H H, Kolkenbrock H J
Adv Exp Med Biol. 1977;86A:187-95. doi: 10.1007/978-1-4684-3282-4_10.
Two new bifunctional reagents suited for the step-wise cross-linking of cysteine and lysine residues in proteins are described. Application to lactate dehydrogenase yields a cross-link between cysteine-165 and lysine-179, which suggests an alternative mechanism by which the "essential" cysteine reacts. For the mapping of the environment of a known and well defined amino acid the use of semireversible bifunctional reagents is suggested.
本文描述了两种适用于蛋白质中半胱氨酸和赖氨酸残基逐步交联的新型双功能试剂。将其应用于乳酸脱氢酶,可在半胱氨酸-165和赖氨酸-179之间形成交联,这表明了“必需”半胱氨酸发生反应的另一种机制。对于已知且明确的氨基酸周围环境的定位,建议使用半可逆双功能试剂。