By Alton Meister
Maintains the authoritative sequence that stories learn into enzymology and similar parts of molecular biology. offers six papers via top professionals.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 56
10-* = KD = PLP affinity high, increased by K + ions ? 10-6 ? 5 91,93, (may bind stable more tight ( K p ~ p= 95% additional PLP 3 . W 5 ) and rapid (k' 115a. = 3700 M. 10-5 (k' = lo00 Mmin-I) 4 1 I 4 2 2 K'Sp) or KPLPvalues were measured under the conditions given; the true affinities at equilibrium ( K D ) are in most cases much higher. 8. 5 (may form aggregates) 6a. DSerine dehydratase ( E . 40 coli) 7. Tryptophanase ( E . coli) 220 liver) 6. L-Serine dehydratase (rat 46 ALEXANDER E. BRAUNSTEIN AND ELIZABETH V.
5) containing 10% glycerol and 1 0 P M PLP b. Chromatography on DEAE167 Sephadex A-50 96 c. 5 saturation d. Filtration through Sephadex G-200 e. 4 " From reference 86. 5) at 23". One U of alliinase produces 1 pmol of pyruvate per minute in this assay system. with 6 M urea, and filtered ohrough Sephadex G-100in a 50 mM phosphate buffer containing 6 M urea and lo-' M KCl, an M, of -65,000 was estimated. The holoenzyme is thus apparently a dimeric protein. Active alliinase preparations contain (per dimer) six equivalents of PLP, which is retained on gel filtration; most of the coenzyme is released on acid denaturation.
In the replacement-specific @-lyases(I, 2 , 4 ) , only a shallow, virnear 415-420 nm is seen in the tually nondichroic band with,,,A absorption spectrum of the free holoenzyme (20). Tolosa). In serine sulfhydrase (2), no spectral change is caused by serine; however, on interaction with cysteine, the 430 nm band is sharpened and shifted slightly to the right (see Fig. 1 1 , from ref. 41). Data concerning the effects of other thiol compounds on this spectral band in lyases 2, 3, and 4 are contradictory and require detailed reinvestigation.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 56 by Alton Meister