Purification, Crystallization and Properties of Tryptophanase fromProteus rettgeri
نویسندگان
چکیده
منابع مشابه
Properties of Crystalline Tryptophanase.
In 1903 Hopkins and Cole (1) identified tryptophan as the source of indole produced by bacterial cultures. The tryptophan-inducible enzyme responsible for this conversion, which is found most commonly in Escherichia coli, was subsequently named tryptophanase by Happold and Hoyle (2). Wood, Gunsalus, and Umbreit (3) showed that tryptophanase catalyzed the stoichiometric conversion of tryptophan ...
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15 صفحه اولThe tryptophanase-tryptophan reaction. 9. The nature, characteristics and partial purification of the tryptophanase complex.
The name tryptophanase was given by Happold & Hoyle (1935) to the enzyme complex of Escherichia coli which induces and catalyzes the production of indole from tryptophan by non-viable bacterial preparations with the consumption of five atoms of oxygen (Woods, 1935). The present communication describes the preparation of this complex in the cell-free state, and subsequent investigation of the co...
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چکیده ندارد.
15 صفحه اولPurification and crystallization of avidin.
An improved purification, including crystallization, of avidin from hen's-egg white is described. The product bound 15.1mug of biotin/mg, corresponding to an equivalent weight of 16200. The amino acid composition showed an integral number of amino acid residues per 16200g, which suggested that each molecule of avidin (mol. wt. approx. 66000) contained four identical subunits.
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1974
ISSN: 0002-1369
DOI: 10.1080/00021369.1974.10861469