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

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.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc278975
Date05 1900
CreatorsMcClure, G. David (George David)
ContributorsCook, Paul F., Harris, Ben G., Sundstrom, Paula, Yorio, Thomas, Easom, Richard, Harris, Elizabeth
PublisherUniversity of North Texas
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
Formatvi, 113 leaves: ill., Text
RightsPublic, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., McClure, G. David (George David)

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