Über die direkte Wirkung von Röntgenstrahlen auf Proteine, Peptide und Aminosäuren
Open Access
- 1 March 1957
- journal article
- research article
- Published by Walter de Gruyter GmbH in Zeitschrift für Naturforschung B
- Vol. 12 (3), 172-180
- https://doi.org/10.1515/znb-1957-0307
Abstract
The primary effect of X-irradiation (2-30 million r) on crystalline lysozyme was investigated by physico-chemical (electro-phoresis, ultracentrifugation), chemical, biochemical and biological methods. A series of closely related, although less basic proteins of different mol. wt. were formed the amino acid constituents of which changed in part into other compounts as a result of irradiation. In amino-and carboxyl-terminal amino acids of the irradiated proteins differences, compared with lysozyme, were found only in the carboxyl terminal groups. The biological activity of the proteins remained practically unchanged even after irradiation with a dose of 5 million r.This publication has 7 references indexed in Scilit:
- DIE ANWENDUNG DER HOCHSPANNUNGSPHEROGRAPHIE BEI DER QUANTITATIVEN TOTALANALYSE VON PROTEINHYDROLYSATEN - UNTERSUCHUNGEN AM LYSOZYM1956
- Energy Requirements for the Inactivation of Bovine Serum Albumin by RadiationRadiation Research, 1954
- Studies on the mechanism of action of ionizing radiations. X. Effect of x-rays on some physicochemical properties of proteinsArchives of Biochemistry and Biophysics, 1952
- The action of X-rays on fibrinogen solutionsArchives of Biochemistry and Biophysics, 1952
- DIRECT CRYSTALLIZATION OF LYSOZYME FROM EGG WHITE AND SOME CRYSTALLINE SALTS OF LYSOZYMEJournal of Biological Chemistry, 1946
- 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
- EFFECTS PRODUCED BY THE IRRADIATION OF PROTEINS AND AMINO ACIDSPhysiological Reviews, 1936