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. 2020 Apr 20;209(4):437–445. doi: 10.1007/s00430-020-00674-2

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© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Immunoprecipitation of 38 kDa protein (Glima 38) by antibodies in sera from patients with type 1 diabetes. Proteins within the rat pancreatic beta-cell line, RIN 5AH, were radiolabelled with ³⁵S methionine by incubation of the cells in medium containing ³⁵S methionine. Proteins were extracted from labelled cells in Triton X-114 and subjected to temperature-induced phase separation to isolate amphiphilic membrane proteins (ref). Radiolabelled membrane proteins were incubated with sera from patients with type 1 diabetes overnight, immune complexes captured on protein A Sepharose, washed and separated by SDS PAGE. The figure shows the results of immunoprecipitation reactions with 16 patients with type 1 diabetes (1–16), two non-diabetic control samples (C), and two Glima 38 positive control samples. Diffuse 38 kDa bands, characteristic of heavily glycosylated membrane proteins such as the tetraspanin family, were specifically immunoprecipitated by antibodies in sera from patients with type 1 diabetes