Ishino S

Noguthi J

Noguchi Junzo

Ishino Shohei

野口 順蔵

石野 昌平

Kanazawa University Repository for Academic Resources

The Science Reports oE the Eanazawa U11iAersity匂 Vol.ITI， No. 1， p. 6:3-65， March， 1955. Studies on the Synthesls of Pl'ute:in Analog'us (Pal't H) Heat necomposition of N-carhothiophenyl回aminoacids長By Shohei ISHINO and ]unzo NOGUCHl (Received Octoher 30， 1954) 63 In the first repo1't1) it was remarked that N-carbothiophenylamino acids expelled thiophenol and carbon dioxide ar吋 werepolymerized in polypεptides ancl this main reaction formed polypeptides， but at the same time the subreactions cal1ed ‘'branched type 円or"ringtype" occured. The thermolysis curves showed that each amino acid had the same tendency of decomposing， b1.1t the tempεr3'tures of the decomposition di佐reda litle according to the kind of amIllo acids. So， in order to investigate the conditions of th町'l1101ysisfurther， we observed the thermolysis curves at the consta11t tempe1'atu1'es of 130oC， 140 uC anc1 150 a11d obtained the activation energy in the main reactions. The samples used are as foIlows : carbothiophenyl-DL-alanyl司glycine，carbothiophenyl-ξ-aminocaproic acid， ca1'bothiophenyl-L-glutamic acid ，carbothiophenyl-L-glutamic acid anhydride， ca1'bothiophenyl--.L-lεucine， carbothiophenyl-DL-a-aminolauric acid， carbo-thiophenyl-DL-alanine， carbothiophenYHj-al託nine，ca1'bothiophenyl-DL-phenylalanine anc1 carbothiophenyl-glycine. AlI of them were prepared by the method discussed in the previous report.1) Taking up about 20 mg. of eaeh sample， we observed the relative curve between the residual sample and the reaction time with the1'mobalance. The results are shown in Fig. 1 Th'Ough no curves completely show linear 同 aotions，the main parts are nearly st1'aight， from which we get the reaction velocity constant K. The relations between log K and 1jT， which乳1'ethe st1'aight lines， a1'e shown in Fig. 2. The activatiol1 energies which a1'e calculated from them are shown il1 Table 1. In the block polymerisations， itis much easier to polyme1'ize glycine， DL-alanine， 戸-alanine，e-aminocaprc止 acid，L-おucineand DL-phe町rlalanine，in which the reactions seem to complete at about 150-160 2) than to polymerise DL-α-aminolau1'ic acid， DL-alanylglycine， L-glutamic acic1 and L-glutamic acid anhydride， il1 which the complete decompositions do not occur unless in a higher tempera組問. 1n such high temperature， itis very dif日cultto obtain the polypeptides having high molecular weights， fo1' the subreactions will occur extensively. There seems to be 10 interrelation between these activation energies and the polymerisabilities of amino acids. 持Itwas published in the Jan. of the Chem. Suciety of Japan 75， 639----640 (1954) (in Japanese). 1) Ja1. of the Chem. Soc. of Japan 7'1， 961 2) J. Noguchi， Jan. of the Chem. Soc. of ]apan 74， 962 (1953) Fig. 2. (10) 20 ↑K4 事由(5) 崎、四hH 、、や抱100 20 (9) 20 150' 20 L耳J!ι一一一」ーo 50 守0--甲骨駆動 t Fig. 1 Thermolysis of N-carbothiophenyl-amino acid at 130'， 140'， 150'Cぜ( 1) Cps-glycine， ( 3 ) Cps-glutamic acid anhydride， ( 5) Cps-glutamic acid， ( 7) Cps-ε-aminocaproic ( 9) Cps-s-alanine， ( 2 ) Cps-DL-phenylalanine， ( 4) Cps-o.-aminolauric acid， ( 6) Cps-DL-喧alanine，( 8) Cps-alanylglycine， (10) Cps-L-leucine Studies on the Synthesisザtrotez"nAnalogus CPart H) 65 ????¥ ¥ -0.6"""2ニトル13Fig.2 Table 1 carbothio向l-a山一"d-I-~~雨戸nergy (Kcal) Glycine 16.13 DL-phenylalanine 16.58 DL-:x-aminolauric acid 21.64 s-alanine 25.54 L-glut耳micacid 25.68 DL-alanine 33.13 L-leωine 33.98 DL-alanyl-glycine 37.03 ε-aminocaproic acid 38 .75 L-glutamic acid anhydride 40 .66 

Studies on the synthesis of Protein Analogus (PartII)

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Studies on the synthesis of Protein Analogus (PartII)

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