New Thiocholine Ester Substrates for the Assay of Human Serum Cholinesterase
نویسندگان
چکیده
منابع مشابه
New thiocholine ester substrates for the assay of human serum cholinesterase.
BACKGROUND Several thiocholine alkanoyl esters were newly synthesized and explored as substrates for the assay of human serum cholinesterase after being subjected to the Ellman reaction (Arch Biochem Biophys 1958;74:443-50 and Arch Biochem Biophys 1959;82:70-7). METHODS We synthesized thiocholine ester iodides by the method of Renshow et al. (J Am Chem Soc 1938;60:1765-70). We examined solubi...
متن کاملComparison between thiocholinesters and o-nitrophenylbutyrate as substrates in the assay of serum cholinesterase.
The technical and clinical usefulnessof three substratesfor serum cholinesterasewere compared. The diagnosticvalue of acetylthiocholine was equal to that of butyrylthiocholine and superior to that of o-nitrophenylbutyrate. Technically, butyryithiocholine is superiorto the other two substrateschiefly becauseof its greater affinity for serum cholinesterase. A kinetic method using o-nitrophenylbut...
متن کاملStructure of human serum cholinesterase.
Human cholinesterase has recently been sequenced and cloned. It is a glycoprotein of 4 identical subunits, each subunit containing 9 carbohydrate chains and 3.5 disuljide bonds. Protein folding is likely to be very similar in human cholinesterase and Torpedo acetylcholinesterase. The cholinesterases have no significant sequence homology with the serine proteases and seem to belong to a separate...
متن کاملOxime reactivation of diethylphosphoryl human serum cholinesterase.
Reactivation of diethyl p-nitrophenyl phosphate inhibited human serum cholinesterase by pyridine-Z-aldoxime methiodide and isonitrosoacetophenone has been investigated as a function of reactivator concentration, pH, and temperature in boric acid-borax buffer and in salt solution. Constants shown were the dissociation constants of the diethylphosphoryl cholinesterase reactivator complex for the ...
متن کاملPurification and properties of human serum cholinesterase.
Cholinesterase was purified from human serum by a three-stage procedure involving chromatography on DEAE-cellulose at pH4.0, an electrofocusing technique and gel filtration on Sephadex G-200. The final product was purified 13000-fold with a yield of 54%, and only one protein and one cholinesterase band could be demonstrated by polyacrylamide-disc electrophoresis. The catalytic properties appear...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Clinical Chemistry
سال: 2001
ISSN: 0009-9147,1530-8561
DOI: 10.1093/clinchem/47.11.1962