Über den Einfluß des Redoxzustandes der löslichen Proteine von Hordeum vulgare auf deren elektrophoretische Trennung in Acrylamid-Gel / Studies in Separation of Soluble Protein from Hordeum vulgare in Acrylamide Gel Columns under the Influence of a Varied Redox State
Open Access
- 1 July 1970
- journal article
- Published by Walter de Gruyter GmbH in Zeitschrift für Naturforschung B
- Vol. 25 (7) , 695-699
- https://doi.org/10.1515/znb-1970-0708
Abstract
The influence of some reducing agents and SH-reagents on the quality of the electrophoretic separation of soluble proteins from barley seedlings in acrylamide-gel was investigated. Admixture of 2-mercaptoethanol or 2,3-dimercaptopropanol produces sharp bands but splits disulfide bonds of the proteins. To avoid this, ascorbic acid together with cysteine can be used as antioxidants. Sulphite or pyrosulphite is unsuitable to protect barley seedling proteins against oxidation. Weakly active oxidizing agents for thiols like arsenite hardly influence the quality of protein separation. Stronger agents, however, for instance H2O2, disturb band formation in the gel columns. Low concentrations of alkylating and mercaptide-forming agents promote the sharpness of the bands. With higher concentrations of SH-reagents derivatives from proteins and arise impede good protein separation in gel columns.Keywords
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