Jadaud P, Thelohan S, Schonbaum G R, Wainer I W
St. Jude Children's Research Hospital, Memphis, Tennessee 38105.
Chirality. 1989;1(1):38-44. doi: 10.1002/chir.530010109.
The stereochemical separation of free and derivatized amino acids on active alpha-chymotrypsin bonded to silica is governed by two mechanisms based on the structure of the solutes or on the enzymatic activity of the enzyme. The deactivation of the hydrolytically active site of the enzyme demonstrated that a significant portion of the retention on this support is due to hydrophobic interactions at other sites. These sites appear to be stereoselective for the ester derivatives of amino acids but not for the other studied solutes.
在键合到硅胶上的活性α-糜蛋白酶上，游离氨基酸和衍生化氨基酸的立体化学分离受两种机制支配，这两种机制基于溶质的结构或酶的酶促活性。酶水解活性位点的失活表明，在这种载体上的保留有很大一部分是由于其他位点的疏水相互作用。这些位点似乎对氨基酸的酯衍生物具有立体选择性，但对其他研究的溶质则没有。
