1954
DOI: 10.1016/s0021-9258(18)71310-0
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Serine Phosphoric Acid From Diisopropylphosphoryl Derivative of Eel Cholinesterase

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Cited by 108 publications
(7 citation statements)
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“…The value of B gives the enzyme concentration directly. 4 A ratio of [S]o/[E]0 = 10 conforms to the requirement of [S] o 13> [E]0 reasonably well. Because of the very high fe/fc3 ratio even values below 10 deviate only slightly (see Fig.…”
Section: + Ks Es]«supporting
confidence: 60%
“…The value of B gives the enzyme concentration directly. 4 A ratio of [S]o/[E]0 = 10 conforms to the requirement of [S] o 13> [E]0 reasonably well. Because of the very high fe/fc3 ratio even values below 10 deviate only slightly (see Fig.…”
Section: + Ks Es]«supporting
confidence: 60%
“…Chymotrypsin, trypsin, papain, acetylcholinesterase, and phosphoglucomutase among others are subject to inhibition by DFP (204,237). When DFP-chymotrypsin is degraded by acid hydrolysis, serine phosphate is obtained (335). Serine phosphate has also been isolated by similar treatment of other enzymes, including trypsin and acetylcholinesterase.…”
Section: Enzymatic Catalysismentioning
confidence: 99%
“…
The amino acid sequence in the region of the reactive serine residue of electric eel (Electrophorus eléctricas) acetylcholinesterase has been determined. The enzyme was inactivated with tritium-labeled pinacolyl methylph o sphonofluoridate, degraded with pepsin, papain, and Pronase, and rganophosphorus anticholinesterases are known (Schaffer et al, 1954) to bind irreversibly the reactive serine residue of electric eel (Electrophorus eléctricas) acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7). In unpublished work of Shaw, it has been reported (Sanger, 1963) that the amino acid sequence in the region of the reactive serine residue in eel acetylcholinesterase is Glu-Ser-Ala.
…”
mentioning
confidence: 99%