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For the experiments described here, we used a modified form of sortase A from Staphylococcus aureus that lacks the first 59 residues, and with the following mutations: E105 K/E108andnd P94R/D160N/D165A/K190E/K196T: Sortase A was produced and purified as described elsewhere.
Bisphenol A was produced from acetone and phenol over an ion-exchange resin catalyst at 50 90°C.
An auxin-like activity due to pteridic acid A was produced by S. hygroscopicus TP-A0451 isolated from Pteridium aquilinum (bracken) stems [116].
Bet v 1.0401 batch A was produced according to previously published methods with minor modifications [12], [13], [14].
Glidobactin A was produced by expression of the homologous plu1881– 1877 gene cluster from Photorhabdus luminescens subsp. laumondii TT01 (Dudnik et al. 2013).
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As this was a low Si/Al molar ratio catalyst, there were three chemical environments for Al confirming that USY-A was produced by a less severe dealumination process in order to achieve a lower Si/Al molar ratio and had not been acid-leached to remove EFAL species, giving it the same Si/Al ratio as via synthesis.
A similar amount of VAL-A was produced in both complemented derivatives JG27/pJTU5287 (2.23 g/L) and JG27/pJTU5288 (2.06 g/L) at 37°C, which accounted respectively for 88.6% and 81.6% of the wild-type yield.
BTX-A is produced by Clostridium botulinum.
VEGF165b, an inhibitory splice variant of VEGF-A, is produced by cultured human podocytes [ 55].
Unlike LDL, Lp (a) is produced in the liver.
The oil, rich in vitamin A, is produced by a large gland in the stomach.
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