Suberimidate crosslinking shows that a rod-shaped, low cystine, high helix protein prepared by limited proteolysis of reduced wool has four protein chains

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Abstract

The cortical cells in a-keratin fibres like wool are filled with microfibrils, composed of proteins with a low cystine content and a high a-helix content, embedded in a matrix of high cystine, zero helix protein [ 11. The microtibril (diam. 7.5 nm) appears to consist of protein subunits regularly arranged in a superhelix [2]. The structure of the subunit is unknown. It has been suggested that it has two [2] or three [2,3] partially a-helical protein chains. A rod-shaped protein (2 X 20 nm) has been prepared from reduced wool by limited trypsin digestion [4,5]. The protein (merokeratin A,) has a low cystine and a high helix content, and therefore it may be a large fragment of the microfibril subunit. The molecular weight of intact, undenatured A 1 measured in the ultracentrifuge, was compared [5] with the molecular weight of the component chains of A1 after denaturation, measured by polyacrylamide gel electrophoresis (PAGE). They were unable to say whether A, had three or four component chains because of uncertainties in both measurements. . Using the dimethyl suberimidate crosslinking technique [6] before denaturation and PAGE, we now show that A, consists of four chains. Therefore, if A, is a fragment of the microfibril subunit, then

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Ahmadi, B., & Speakman, P. T. (1978). Suberimidate crosslinking shows that a rod-shaped, low cystine, high helix protein prepared by limited proteolysis of reduced wool has four protein chains. FEBS Letters, 94(2), 365–367. https://doi.org/10.1016/0014-5793(78)80978-8

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