Year: 1955
Type: article
Abstract: taken into account when considering possible configurations for the polypeptide chain in this area.It is interesting that the ring is the same size as the similar disulphide ring found in oxytocin (Tuppy & Michl, 1953; du Vigneaud, Ressler & Trippett, 1953) and vasopressin (Acher & Chauvet, 1953; du Vigneaud, Lawler & Popenoe, 1953), which suggests that it may have a possible structural or biological significance.SUMMARY 1. Insulin was subjected to partial hydrolysis with chymotrypsin, with a crude pancreatic extract and with acid under conditions in which the di- sulphide bonds were stable.2. Cystine-containing peptides in the hydroly- sates 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 separa- tions.3. From the structure of the cystine peptides the distribution of the disulphide bonds of insulin was deduced and is shown in Table 10.A. P.R.
Source: Biochemical Journal
DOI: 10.1042/bj0600556
Authors: H. Brown, F. Sanger, Ruth Kitai
Institution: University of Cambridge
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1875728332