000			01626nam a2200253Ia 4500
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005			20250625153947.0
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090			_aB-14744
245	1	0	_aCloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Eschericha coli
490	0		_vGene, 18, p.1-12, 1982
520	3		_aThe structural gene of the sweet-tasting plant protein (prepro)thaumatin was cloned and expressed in Escherichia coli. Expression was effected under control of fuc and trp promoter/operator systems and through the use of bacterial ribosome-binding sites. The naturally occurring thaumatin II represents a processed form. The primary translation product, preprothaumatin, of the cloned mRNA-derived cDNA contains extensions at both the amino terminus and the carboxy terminus. The amino terminal extension of 22 amino acids is hydrophobic and very much resembles an excretion-related signal sequence. The six amino acids-long carboxy terminal extension is very acidic in character, in contrast to the overall highly basic thaumatin molecule. The possible role of such an acidic tail with respect to compartmentalization is discussed.
700	1	2	_aEdens, L.
700	1	2	_aHeslinga, L.
700	1	2	_aKlok, R.
700	1	2	_aLedeboer, A.M.
700	1	2	_aMaat, J.
700	1	2	_aToonen, M.Y.
700	1	2	_aVisser, C.
700	1	2	_aVisser, C.
856	4	0	_uhttps://drive.google.com/file/d/1SvWqJWe2473Ql2dOzElGibHc9zb1ynAl/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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