Kristallisierte Leucinaminopeptidase aus Rinderaugenlinsen. Physikalische Konstanten, II. Hydratationsgrad und Gestaltsbestimmung mit hydrodynamischen Methoden
- 1 January 1967
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 348 (Jahresband) , 1158-1162
- https://doi.org/10.1515/bchm2.1967.348.1.1158
Abstract
The viscosity increment (v[image] = 5.08) were determined for leucine aminopeptidase from bovine lens. For the maximal degree of hydration, wmax was 0.257 g. water/g. protein. From these values and the friction ratio, it is possible to calculate the limits of probability for the ratio of the axes a/b, assuming a compact rotational elipsoid. An prolated form gives the values 3.0[less than or equal to] a/b [less than or equal to]4.0, and an oblated form gives 0.23 [less than or equal to] a/b [less than or equal to] 0.31. The effect of anomalies of shape on the axes ratio measured by hydrodynamic methods, and a correction of the axes ratio for zero degree of hydration (w = 0 g. water/g. protein) are discussed. The partial specific volumes determined earlier by pyknometric methods are confirmed by the partial specific volumes of the amino acid residues, which are calculated from the amino acid composition.This publication has 3 references indexed in Scilit:
- Reihenbestimmungen von Stickstoff im Ultramikromaßstab. Kjeldahlveraschung und Phenol-Hypochlorit-ReaktionHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1967
- Zur Darstellung und Substratspezifität einer von der Leucinamino-peptidase unterscheidbaren Aminopeptidase aus NierenpartikelnHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1967
- An upper limit to the amount of hydration of a protein molecule A corollary to the “limiting law of protein structure”Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1965