SYNTHESIS OF THE PEPTIDE FRAGMENTS OF THE B-CHAIN OF INSULIN——Ⅴ.STUDIES ON THE SYNTHESIS AND DEGRADATION OF A DERIVATIVE OF THE C-TERMINAL DECAPEPTIDE OF THE B-CHAIN OF INSULIN
SYNTHESIS OF THE PEPTIDE FRAGMENTS OF THE B-CHAIN OF INSULIN——Ⅴ.STUDIES ON THE SYNTHESIS AND DEGRADATION OF A DERIVATIVE OF THE C-TERMINAL DECAPEPTIDE OF THE B-CHAIN OF INSULIN作者机构：Institute of Biochemistry Academia Sinica Shanghai
出 版 物：《Science in China,Ser.A》 (中国科学A辑(英文版))
年 卷 期：1963年第9期
页 面：1321-1332页
主 题：OCH SYNTHESIS OF THE PEPTIDE FRAGMENTS OF THE B-CHAIN OF INSULIN STUDIES ON THE SYNTHESIS AND DEGRADATION OF A DERIVATIVE OF THE C-TERMINAL DECAPEPTIDE OF THE B-CHAIN OF INSULIN
摘 要：Carbobenzoxy-r-methylglutamylnitroarginylglycylphenylalanylphenylalanyltyrosylthreonylprolyl （etosyl） lysylalanine methyl ester (B21-30), a derivative of the C-terminal decapeptide of the B-chain of insulin, has been prepared by coupling carbobenzoxy-r-methylglutamylnitroarginine with glycyl-phenylalanylphenylalanyltyrosylthreonylprolyl （e-tosyl） lysylalanine methyl ester by the carbodiimide method. The dipeptide derivative has been prepared by condensing nitroarginine with p-nitrophenyl carbobenzoxy-r-methyl glutamate while the octapeptide ester has been obtained from carbobenzo-xyoctapeptide methyl ester by catalytic hydrogenolysis. Saponification of the protected decapeptide ester gave rise to carbobenzoxyglutamylnitroarginylglycylphenylalanylphenylalanyltyrosylthreonylprolyl （e-tosyl） lysylalanine (B21-30a) which could be completely digested by kidney carboxypeptidase. The finding that only alanine was liberated from the protected decapeptide by the action of pan creatic carboxypeptidase, in accord with the results of the synthetic protected octapeptide as well as the B-chain of insulin, further proved the homogeneity of the product. N Tosylated free decapeptide could be obtained from the protected decapeptide (B21-80a) by prolonged catalytic hydro-genolysis while the same treatment on the protected decapeptide ester gave rise to the decapeptide ester as well as some of its cyclized product, which presumably resulted from the former by condensation of the a-amino with the r-methyl ester group. The readiness of such cyclization into the pyrollidone derivative could be greatly enhanced by prolonged standing at 30℃ in slightly acidic medium, brief heating of the aqueous solution or chromatography with an ammonia-butanol solvent system. All decapeptide derivatives despite the presence or absence of the a-amino group but with the guanidino group free could be completely hydrolyzed by trypsin into di-and octa-peptide derivatives. This finding further verified the opti
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