Über kininliefernde Peptide aus pepsinverdauten Rinderplasmaproteinen
- 1 January 1967
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 348 (Jahresband) , 177-182
- https://doi.org/10.1515/bchm2.1967.348.1.177
Abstract
Two low molecular weight peptides were isolated after the digestion of bovine plasma proteins with pepsin. After treatment with kallikrein, they gave, respectively, the N-terminal dipeptides Ser-Arg or Gly-Arg and methionylkallidin. Bradykinin was released by the action of tryp-sin. The kinin sequence of these low molecular weight kininogens is situated at the carboxyl end, since kinin can no longer be released after the action of carboxypeptidase B. It was also shown that undigested plasma contains 2 different high molecular weight kininogens with protected and free C-terminal kinin sequences; only 60% of the kinin is released after the action of carboxypeptidase B.This publication has 3 references indexed in Scilit:
- Strukturaufkl rung kininliefernder Peptide aus Rinderserum-KininogenNaunyn-Schmiedebergs Archiv für experimentelle Pathologie und Pharmakologie, 1966
- Methionyl-lysyl-bradykinin, a new kinin from ox bloodBiochemical Journal, 1965
- Preparation and Properties of Serum and Plasma Proteins. IV. A System for the Separation into Fractions of the Protein and Lipoprotein Components of Biological Tissues and Fluids1a,b,c,dJournal of the American Chemical Society, 1946