%0 Journal Article
%T Separation of alpha-amino acids and peptides by chelated metal ion affinity chromatography]<br>螯合金属离子亲和色谱法分离α-氨基酸和肽
%A H Cheng
%A T Shao
%A <br>程慧文
%A 邵天梦
%J 色谱
%D 1997
%I 
%X The hydrolytic solution of proteins mainly contains free amino acids and peptides. The separation of amino acids and di- and tri-peptides is very significant and also a complicated work. This report presents a chelated metal ion affinity chromatographic (CMAC) method for the separation of alpha-amino acids and peptides. Sephadex G10 was used as the solid matrix. It was epoxy-activated by epichlorophydrin; then coupled with iminodiacetate (IDA) and chelated with copper ion to produce immobilized copper-ion affinity chromatographic packing. Some examples are given for the chromatography of model mixtures of L-Val, L-His, L-Tyr, L-Try, Tyr-Try dipeptides and protein hydrolyzing solution of fish. The separation was based on the different stabilities of copper complexes of alpha-amino acids, peptides and IDA-Sephadex G10. The components which form weak complexes with copper apparently move along with the solvent front. Alpha-amino acids-copper complexes with a stability comparable to that of copper-IDA-Sephadex G10 are retained on the matrix. Peptides form strong complexes and catch copper from the matrix. They are only slightly retained. The results showed that alpha-amino acids and peptides were completely separated under the experimental conditions.
%K NULL<br>螯合金属离子
%K 亲和色谱法
%K 氨基酸
%K 肽
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=6E709DC38FA1D09A4B578DD0906875B5B44D4D294832BB8E&cid=6579068328FE643F&jid=4D81E042D77AFEC6881D14759692069C&aid=A0C7CB2C65AD7C6D24D6A788E07B93C2&yid=5370399DC954B911&vid=23CCDDCD68FFCC2F&iid=94C357A881DFC066&sid=EB58C3052341AAA3&eid=8CCD0401CC9AE432&journal_id=1000-8713&journal_name=色谱&referenced_num=1&reference_num=1