Abstract
After recent discoveries of bovine, porcine, rat and human proinsulin, extensive efforts have been made for their physiological and biological significance. Only a few informations are available concerning them at present, because of shorter quantity of the hormones.
An isolation method of porcine proinsulin from crystalline porcine insulin with easy performance has been described.
Repeated gel chromatographic separations of porcine insulin on Bio-Gel column yielded crude porcine proinsulin and its intermediate form. A single band component with corresponding electrophoretic mobility of porcine proinsulin was obtained by linear gradient chromatography of this crude material on DEAE-cellulose column, and was converted to insulin by trypsin digestion. All of DEAE-cellulose chromatographic fractions having more basic components than insulin could be converted to insulin by the trypsin treatment. Amino acids analysis of this single band component appeared to be the same amino acids composition of known porcine proinsulin.
