. Ciba Foundation Symposium on the Regulation of Cell Metabolism. Cell metabolism. 190 Phillips W. Robbins and Fritz Lipmann strongly marked in the absence of CoA, indicating a prevalence of glycolytic breakdown in the latter case. We were rather interested in the radioactive spot below the lactic acid which appears strongly in the CoA-containing sample, until it was identified as phospho- glycerol. The appearance of this compound under these conditions may be of interest but we did not wish to expand on this observation. When we came to test insulin in this system, it proved to be. 5 10 15 20
. Ciba Foundation Symposium on the Regulation of Cell Metabolism. Cell metabolism. 190 Phillips W. Robbins and Fritz Lipmann strongly marked in the absence of CoA, indicating a prevalence of glycolytic breakdown in the latter case. We were rather interested in the radioactive spot below the lactic acid which appears strongly in the CoA-containing sample, until it was identified as phospho- glycerol. The appearance of this compound under these conditions may be of interest but we did not wish to expand on this observation. When we came to test insulin in this system, it proved to be. 5 10 15 20 Coenzyme A - units/ml. 25 Fig. 2. Effect of CoA concentration on glucose incorporation into glycogen and on the maintenance of glycogen. Incubations were carried out for 60 minutes as described by Robbins, Traut and Lipmann (1959) and in Fig. 1. The reactions were stopped by adding an equal volume of 60 per cent KOH. Glycogen was isolated for counting and for chemical glycogen determinations essentially by the method described by Hassid and Abraham (1957). completely inactive. Adrenaline, at a relatively high concentration, inhibits glucose incorporation into glycogen. We come now to the results which have impressed us most, and which bear on the relationship bet^\ 3n phosphorylase and glycogen synthesis. The experiment traced in Fig. 4 was carried out to explore the effect that an increase in phosphorylase a by addition of phosphorylase kinase might have on glycogen synthesis. It appears that an addition of kinase which maintains phosphorylase a at a higher level, almost completely abolishes glucose incorporation. In contrast, in the absence of kinase, the steady decrease in phos- phorylase activity to practically zero coincides rather startlingly with an increase of glucose incorporation into glycogen. In Fig. 5,. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these ill
Size: 2077px × 1203px
Photo credit: © Library Book Collection / Alamy / Afripics
License: Licensed
Model Released: No
Keywords: ., bookcentury1900, bookcollectionb, bookpublisherbostonlittlebrown
