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All Rights Reserved. Under the terms of the licence agreement, an individual user may print out a PDF of a single chapter of a monograph in OSO for personal use (for details see Abstract and Keywords This chapter seeks to contribute to an indexical theory of style by demonstrating how the relationship between stance, style, and identity is formed both from(More)
A growing body of discourse-analytic studies demonstrates that within the legal system, spoken language that undergoes entextualization is transformed in a variety of sociopolitically consequential ways. Through the analysis of a legal case involving the institutional entextualization of incriminating language—an FBI summary log of wiretapped telephone(More)
and an anonymous referee for insightful feedback on this work. We also thank our speakers and participants for their invaluable contributions to this research. Any remaining errors and omissions are our own. What motivates a fluent bilingual speaker to switch languages within a single utterance? We propose a novel discourse-functional motivation: less(More)
Acetyl-coenzyme A: 13-sophorosyloxydocosanoic acid (Glc2HDA) acetyltransferase was purified 14-fold in low yield from Candida bogoriensis cells. The enzyme catalyzes acetylation of the 6' and 6" positions of the sophorosyl group, producing the 13-[2'-O-beta-D-glucopyranosyl-beta-D-glucopyranosyloxy]-docosanoic acid 6',6"-diacetate (Ac2Glc2HDA) and(More)
The commitment of sociocultural linguistics to the cause of social justice has been central to the discipline since its foundation. This commitment is nowhere more evident than in the educational domain and particularly in the development of sociolinguistically informed curricula and teacher preparation programs. Such programs help ensure that students who(More)
Two enzymes have been isolated from Candida bogoriensis which catalyze the hydrolysis of 13-sophorosyloxydocosanoic acid (Glc2HDA) esters obtained from this organism. The 6',6"-diacetyl derivative of Glc2HDA (Ac2Glc2HDA) is hydrolyzed by an acetylesterase (EC 3.1.1.6) which has been purified 1300-fold. The acetylesterase has a molecular weight of 35,000(More)
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