Tylosin rapid test strip (Egg) (DTS1028L)

Regulatory status: For research use only, not for use in diagnostic procedures.

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Intended Use
Tylosin rapid test strip is developed for rapid test of tylosin contamination in egg.
The kit can be stored at room temperature (2-30°C). The test kit is stable through the expiration date marked on the foil pouch. DO NOT FREEZE. Do not store the test kit in direct sunlight.
The sensitivity of tylosin residues in egg is 50 ppb.
General Description
Tylosin is an antibiotic of the macrolide class (same class as erythromycin). It is made naturally by the bacterium Streptomyces fradiae and acts to inhibit bacterial protein synthesis by inhibiting the 50S ribosome, a cellular structure only certain bacteria have and use to make internal proteins.


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Impact of a Natural Feed Additive or Tylosin on Finishing Beef Cattle Performance and Liver Abscess Rate.


Authors: Wilson, H. C.; Hilscher, F. H.; Boyd, B. M.; MacDonald, J. C.; Erickson, G. E.

Exploring the molecular basis for substrate specificity in homologous macrolide biosynthetic cytochromes P450


Authors: DeMars, Matthew D., II; Samora, Nathan L.; Yang, Song; Garcia-Borras, Marc; Sanders, Jacob N.; Houk, K. N.; Podust, Larissa M.; Sherman, David H.

Cytochromes P450 (P450s) are nature's catalysts of choice for performing demanding and physiologically vital oxidation reactions. Biochemical characterization of these enzymes over the past decades has provided detailed mechanistic insight and highlighted the diversity of substrates P450s accommodate and the spectrum of oxidative transformations they catalyze. Previously, we discovered that the bacterial P450 MycCI from the mycinamicin biosynthetic pathway in Micromonospora griseorubida possesses an unusually broad substrate scope, whereas the homologous P450 from tylosin-producing Streptomyces fradiae (TylHI) exhibits a high degree of specificity for its native substrate. Here, using biochemical, structural, and computational approaches, we aimed to understand the molecular basis for the disparate reactivity profiles of these two P450s. Turnover and equilibrium binding experiments with substrate analogs revealed that TylHI strictly prefers 16-membered ring macrolides bearing the deoxyamino sugar mycaminose. To help rationalize these results, we solved the X-ray crystal structure of TylHI in complex with its native substrate at 1.99-? resolution and assayed several site-directed mutants. We also conducted molecular dynamics simulations of TylHI and MycCI and biochemically characterized a third P450 homolog from the chalcomycin biosynthetic pathway in Streptomyces bikiniensis. These studies provided a basis for constructing P450 chimeras to gain further insight into the features dictating the differences in reaction profile among these structurally and functionally related enzymes, ultimately unveiling the central roles of key loop regions in influencing substrate binding and turnover. Our work highlights the complex nature of P450/substrate interactions and raises interesting questions regarding the evolution of functional diversity among biosynthetic enzymes.

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