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GrainGenes Reference Report: JCS-17-203

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Reference	JCS-17-203
Title	Functional properties of low Mr wheat proteins. I. Isolation, characterization and comparison with other reported low Mr wheat proteins
Journal	Journal of Cell Science
Year	1993
Volume	17
Pages	203-220
Author	Prieto J Weegels P Hamer R
Abstract	A group of low Mr wheat proteins with characteristic extractability behaviour was isolated using two different isolation procedures The proteins were extractable with water, salt solution and 70% (v/v) ethanol After water extraction of flour and separation of gluten, a substantial proportion of these proteins was still extractable from gluten using 70% (v/v) ethanol Based on their amino acid compositions, M(r)s and IEF patterns, the isolated proteins resemble closely most of the alpha-amylase/protease inhibitors described in the literature This was confirmed by enzyme inhibition studies in which it was shown that they inhibited mammalian, but not wheat, bacterial and fungal alpha-amylases All proteases tested were inhibited by the low M(r) proteins. Their M(r)s and their high cysteine contents (6.5-8.1 mol%) indicated that the proteins contain four to five disulphide bonds. Free thiol groups were not detected in the proteins. Upon reduction, the M(r) increased from 7-8000 to 14-19000. Furthermore, the disulphide bonds were highly reactive as determined by their reaction with the thiol-specific label monobromobimane. This suggests that the low M(r) wheat proteins may play a role in thiol group/disulphide bond exchange in wheat proteins.
Keyword	characterization [ Show all 6 ]

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