A Study of the Intrinsic Fluorescence of O-Acetyl-L-Serine Sulfhydrylase-A from Salmonella typhimurium

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O-Acetyl-L-serine sulfhydrylase-A (OASS-A) forms acetate and L-cysteine from O-acetyl-L-serine (OAS) and sulfide. One molecule of the cofactor pyridoxal 5'- phosphate (PLP) is bound in each holoenzyme protomer.

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vi, 113 leaves: ill.

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McClure, G. David (George David) May 1993.

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  • McClure, G. David (George David)

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O-Acetyl-L-serine sulfhydrylase-A (OASS-A) forms acetate and L-cysteine from O-acetyl-L-serine (OAS) and sulfide. One molecule of the cofactor pyridoxal 5'- phosphate (PLP) is bound in each holoenzyme protomer.

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vi, 113 leaves: ill.

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  • May 1993

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  • March 26, 2014, 9:30 a.m.

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  • March 27, 2020, 7:59 a.m.

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Thumbnail image of item number 1 in: 'A Study of the Intrinsic Fluorescence of O-Acetyl-L-Serine Sulfhydrylase-A from Salmonella typhimurium'.
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McClure, G. David (George David). A Study of the Intrinsic Fluorescence of O-Acetyl-L-Serine Sulfhydrylase-A from Salmonella typhimurium, dissertation, May 1993; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc278975/: accessed May 26, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .

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