The disulphide bonds of insulin

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Abstract
Insulin was subjected to partial hydrolysis with a crude pancreatic extract and with acid under conditions in which the disulfide bonds were stable. Cystine-containing peptides in the hy-drolysates were separated and their structure determined after oxidation to cysteic acid peptides. Paper ionophoresis at high potential gradients in pyridine-acetic acid buffers was found useful for the separations. From the structure of the cystine peptides the distribution of the disulfide bonds of insulin was deduced and is shown.