Biotin bioavailability from poultry and swine feed ingredients was determined in an experiment involving growing rats (55-60 g body weight, initially), housed individually in stainless steel cages with raised metal floors. The rats were fed a biotin-free diet fortified with egg-white powder for 7 d prior to being put on test. Thereafter, 5 rats were randomly assigned to each of the experimental diets, as follows: a basal egg white-free diet (A) without added biotin, or supplemented with graded levels of d-biotin, i.e., 0.05, 0.10, 0.25, 0.50 and 1.00 microgram/g, and also 12 test diets prepared by incorporating various cereal grains and/or two protein supplements into diet A by partial replacement of casein and carbohydrates. The experimental diets were fed ad libitum for 21 d, and met or exceeded recommended levels for all nutrients except biotin. Results showed significant correlations between pairs of parameters, including plasma biotin vs biotin intake (P less than 0.01), liver biotin vs biotin intake (P less than 0.05) and plasma biotin vs liver biotin (P less than 0.01). The bioavailable biotin from test ingredients was estimated using the derived regression equation, Y = 0.54X + 1.05, (r = 0.85), where X = biotin intake (microgram/d) and Y = plasma biotin (ng/ml). In most cases, these values were greater than the corresponding biotin intakes, indicating that intestinal biotin synthesis and coprophagy might be increasing the supply of bioavailable biotin to the rats. Therefore, the rat might not be a good model animal for routine evaluation of biotin bioavailability from feed ingredients.(ABSTRACT TRUNCATED AT 250 WORDS)
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J Med Chem
January 2025
Department of Medicinal Chemistry, University of Minnesota, 308 Harvard Street SE, Minneapolis, Minnesota 55455, United States.
The antibacterial agent Bio-AMS is metabolized in vivo through hydrolysis of the central acyl-sulfamide linker leading to high clearance and release of a moderately cytotoxic metabolite . Herein, we disclose analogues designed to prevent the metabolism of the central acyl-sulfamide moiety through steric hindrance or attenuation of the acyl-sulfamide electrophilicity. was identified as a metabolically stable analogue with a single-digit nanomolar dissociation constant for biotin protein ligase (BPL) and minimum inhibitory concentrations (MICs) against and ranging from 0.
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Department of Nutrition, Faculty of Veterinary Medicine, Firat University, Elazig, Turkey.
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Department of Rheumatology, Leiden University Medical Center, Leiden, The Netherlands.
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Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
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View Article and Find Full Text PDFAnal Chem
January 2025
College of Chemistry, Central China Normal University, 152 Luoyu Road, Wuhan 430079, China.
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