The action pattern of potato phosphorylase
- 1 December 1954
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 58 (4) , 560-569
- https://doi.org/10.1042/bj0580560
Abstract
The action pattern of potato phosphorylase has been shown to be completely multi-chain both in the synthesis and the phosphorolysis of amylose. Synthetic amyloses of known average chain length have been prepared and, up to 160, their degrees of polydispersity (deter- mined by Mould and Synge, 1954) are shown to be entirely in agreement with values calculated on the assumption of multi-chain action. The priming activities of the maltodextrins have been compared. Maltotriose is the lowest memeber of the series to exhibit priming activity. This activity is very weak and the higher members, malto-tetraose, -perttaose and -hexaose are much more efficient.Keywords
This publication has 9 references indexed in Scilit:
- Separations of polysaccharides related to starch by electrokinetic ultrafiltration in collodion membranesBiochemical Journal, 1954
- Products of the β-amylolysis of maltodextrinsBiochemical Journal, 1954
- D-Enzyme: a Disproportionating Enzyme in Potato JuiceNature, 1953
- The coupled oxidation of pyruvate with glutathione and cysteineBiochemical Journal, 1951
- INTRAMOLECULAR NATURE OF THE OXIDATIVE INACTIVATION OF CRYSTALLINE BETA-AMYLASE1951
- PHYSICOCHEMICAL STUDIES ON BETA-AMYLASE1950
- Sur les enzymes amylolytiques VII. L'isophosphorylase et la formation de polysaccharides ramiflésHelvetica Chimica Acta, 1948
- The reversible formation of starch from glucose-1- phosphate catalysed by potato phosphorylaseProceedings of the Royal Society of London. B. Biological Sciences, 1940
- The estimation of phosphorusBiochemical Journal, 1940