No abstract

Insulins from mouse and spiny mouse have been extracted with acid ethanol and purified by gel filtration and chromatography on CMcellulose. Two different mouse insulins could be separated by gel electrophoresis. The amino acid compositions of mouse insulins 1 and II and of their constituent chains were found to be identical with the ones of rat insulins 1 and 11. In Acomys, a single insulin was found. The amino acid compositions of two different Acomys strains (black and yellow, resp.) were found to be identical.The amino acid composition of A chain is the same as in rat and mouse insulin A chain, whereas the one of B chain is the same as in rabbit insulin B chain. Studies using digestion with aminopeptidase and with trypsin are in accord with the assumption that the A chain sequence is identical to the one of rat A chain, and that the chain is identical to the one of rabbit chain. Biological activities of mouse and Acomys insulins are within the normal range. No indication of an "abnormal" insulin in Acomvs has been found. Isolierung und partielle Slruktitraufklärnng von Insulin aus der Maus (Mus musculus) und der S t ache lmaus (Acomys cahirinus)