VOL. 12 (1953) SOLUBLE NITROGEN FRACTION IN PEA PLANT AND AI.DKR 185 



Fig. I A"D shows [)aper chromatograms of these hydrolysates. x^s can be seen from 

 them no amino acids were hberated by i h hydrolysis. In the chromatogram of the 3 h 

 hydrolysate wide indefinite spots were formed, thus amino acids, possibly liberated 

 to a small extent, were difficult to identify. Perhaps some homoserine, serine, glycine, 

 glutamic acid, proline, and aspartic acid were liberated. Not until in the total hydrolysis 



i'ALYSAHLE , 

 Dial vSA'&L B Mild HYDgDivii^ 



(ih.ur IN HCl,K)0°t) 



^^ ''"^ ■ f Ho -1335- ? t. 



[( 



•■# 





D/alvsaBLB, ; 



(3 houn, 1-N HCL, % J „„ 



lOO'C). 



TOTAL HYDROi-ySlS 



Fig. I. Dialysable "peptides", not hydrolysed and the same after mild and strong hydrolysis. For 

 solvents and technique see^^or 1^. i = gly, 2 = ala, 3 = val, 7 = tyr, 8 = ser, 9 = thr, 11 = pro, 

 14 = arg, 15 = lys, 16 = asp. ac, 17 = glu. ac, 29 = }'-AB, 32 = ^-ala, 45 = ethanolamine, 51 = 



homoserine, "S" and "W" = unknown spots. 



were all the amino acids liberated and the unclear spots disappeared. The results of the 

 hydrolysis suggest that at least a major part of the amino acids have been bound by 

 difficultly hydrolyzable bonds. Our experiments on the hydrolysis of acetyl glucosamine 

 have shown that acetyl group is split off from it as soon as within i h hydrolysis with 

 I N HCL Thus no acetylamino acids should be f)resent in our "peptide" fraction. 



An interesting question is the manner of combination in the "peptide" fraction of 

 such amino acids as homoserine, y-AB, and /3-alanine, which are liberated in the acid 



References p. i8y. 



