Über die enzymatische Spaltbarkeit der Prolin‐Peptide. (Vorläuf. Mitteil.)

Abstract

192933 Grassrnann, D y c k e r h o jf , 21. Xc h o e n e b e c k. I307 Eine 1.g3-proz. Losung in Wasser, von der Dichte I .oo 53 zeigte im I-dm-Rohr eine Rechtsdrehung von 0.46O, woraus sich [u]: zu + ~3 . 7 4~ berechnet. Ganz das gleiche Produkt resultjerte beim erschopfenden M e t h y l i e r e n d e s D i h y d r o -c a m p h y l a m i n s in der auf S. I305 beschriebenen Weise. Das Praparat (gef. 39.25J) schmolz Lei 27S0 und drehte in 2.08-proz. waoriger Losung von der Dichte 1.0056 im 1-dm-Rohr 0 . 5~ nach rechts, woraus sich [ c c : : zu +z3.9zo ergiht. 199. W. G r a s s m a n n , H. D y c k e r h o f f und 0 . v. S c h o e n e b e c k : Ober die enzymatische Spaltbarkeit der Prolin-Peptide. (Vorlauf. Mitteil.) [Aus d. Chem. Laborat. d. Bayer. Akadem. d. Wissenschaften in Miinchen.]Die in den letzten Jahren durch H. v. E u l e r und K. Josephsonl),

The Specificity of Certain Peptidases

“…rather than by prolidase (44). The hydrolysis of L-prolylglycine has been attributed by Grassmann and co-workers (95,96) to another enzyme, prolinase; most of the prolinase activity is easily removed during the purification of prolidase (44). It is likely that the hydrolysis of hydroxy-L-prolylglycine is also due to prolinase (44).…”

The Enzymatic Properties of Peptidases

“…(22) found that dried erepsin preparations split leucylglycine but not prolylglycine, whereas fresh solutions split both substrates. They, therefore, postulated a "prolinasc" distinct from "dipeptidase."…”

Aminopeptidases in the Acidic Fraction of the Yeast Autolysate

“…5 ) APases in yeast were first described by Grassmann et al [6][7][8] Thereafter, 10hnson 9 ) purified another APase (aminopolypeptidase) from Saccharomyces cerevisiae as a single protein, the molecular weight of which was 670,000. However, the APases which we found seemed to differ from the known ones.…”