THE THERMAL CONDENSATION OF GLUTAMIC ACID AND GLYCINE TO LINEAR PEPTIDES
THE THERMAL CONDENSATION OF GLUTAMIC ACID AND GLYCINE TO LINEAR PEPTIDES
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DOI:
10.1021/ja01544a027
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发表时间:
1958-01-01
影响因子:
15
通讯作者:
FOX, SW
中科院分区:
文献类型:
--
作者:
HARADA, K;FOX, SW
Although glutamic acidis convertedby heat virtually entirely to the inner lactam, it undergoes copolymerization with each of many amino acidsto yield linear peptides. The effects of conditions of reaction have been studiedfor the copolymerization of glutamic acid and glycine. The dialyzed products, of average molecular weight 11,000-20,000, have also been characterized in yield, amino acid composition, N-terminal amino acid composition and infrared absorption spectra.The heating of unsubstituted amino acids has typically yielded diketopiperazines, decarboxylation products and tars rather than linear peptides. 2-4 Such experiments have been carried out with single amino acids in almost all cases. When, however, amino acids are copolymerized by heat, 5 there often result linear peptides from amino acids which fail to yield peptides when heated individ-ually. 6 Continuing investigation reveals differ-ent patterns of behavior for different combinations of amino acids. In this paper is described the formation of copolymers of glutamic acid and gly-