Inaktivierung der Kaninchen‐muskel‐und‐leberaldolase in 4M Harnstofflösung. Über Aldolasen, 6. Mitteilung
- 1 January 1965
- journal article
- research article
- Published by Wiley in Helvetica Chimica Acta
- Vol. 48 (7) , 1546-1555
- https://doi.org/10.1002/hlca.19650480715
Abstract
(1) Muscle and liver aldolase from rabbit are reversibly inactivated in 4M urea at pH 7,6, without being split into sub‐units. At the same pH value muscle aldolase, but not liver aldolase, dissociates into three sub‐units, if the ionic strength is increased by the addition of NaCl to a final concentration of 0,2M. At pH 5,5 and low ionic strength (in the absence of NaCl) both aldolases dissociate into sub‐units.This publication has 30 references indexed in Scilit:
- Über die Aldolase der Kaninchenleber: Molekulargewicht, Dissoziation in Untereinheiten. Über Aldolasen, 5. MitteilungHelvetica Chimica Acta, 1965
- The unfolding and refolding of ribonuclease in urea solutionsJournal of Molecular Biology, 1964
- Isothermal Unfolding of Globular Proteins in Aqueous Urea SolutionsJournal of the American Chemical Society, 1964
- Correlation of Structure and Function in Enzyme ActionScience, 1963
- Enymic Homology. Structural and Catalytic Differentiation of Fructose Diphosphate Aldolase.Acta Chemica Scandinavica, 1963
- Kristallisation einer Aldolase aus KaninchenleberHelvetica Chimica Acta, 1963
- Bedeutung von SH-Gruppen für die enzymatische Aktivität. Studien an Milchsäuredehydrogenase aus SchweineherzArchives of Biochemistry and Biophysics, 1959
- An Ultracentrifuge Study of the Polymerization of α-ChymotrypsinJournal of the American Chemical Society, 1958
- Über Aldolasen. 1. Mitteilung. Kristallformen und Aktivität der MuskelaldolaseHelvetica Chimica Acta, 1957
- ORGANIZATIONAL CONSTRUCTS: AN APPROACH TO UNDERSTANDING ORGANIZATIONS.Academy of Management Proceedings, 1956