Alkaline Phosphatase: IHC Dephosphorylation for Rapid Cancer Detection
نویسندگان
چکیده
منابع مشابه
Dephosphorylation of phosphoproteins by Escherichia coli alkaline phosphatase.
A purified commercial preparation of Escherichia coli alkaline phosphatase (EC 3.1.3.1) has been shown to dephosphorylate several phosphoproteins including bovine heart glycogen synthase D, mixed phosphohistones, and rabbit skeletal muscle phosphorylase kinase but not rabbit skeletal muscle glycogen phosphorylase. Alkaline phosphatase completely removed phosphate groups previously added during ...
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S ERUM ALKALINE PHOSPHATASE ACTIVITY is the enzyme analysis most frequently made in clinical laboratories. It has long been a diagnostic tool and therapeutic index in both liver and osseous disease. Its usefulness could be expanded by a method which would measure alkaline phosphatase activity rapidly, accurately, and with a minimum of technical manipulation. Ideally, the substrate for such a me...
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A novel ferrocene-derived substrate for the ratiometric electrochemical detection of alkaline phosphatase (ALP) was designed and synthesised. It was demonstrated to be an excellent electrochemical substrate for the ALP-labelled enzyme-linked immunosorbent assay (ELISA).
متن کاملDetection of alkaline phosphatase/immunoglobulin complexes.
We report another patient with a circulating alkaline phosphatase/immunoglobulin complex in his blood, and describe a simple method of demonstrating such complexes. On electrophoresis on cellulose acetate, the complex was relatively slow moving and there was no activity in the normal bone/liver isoenzyme region. When the serum was treated with trypsin, the slow band disappeared and the normal p...
متن کاملPresteady State Kinetics of Phosphoro - thioate Hydrolysis by Alkaline Phosphatase RATE - LIMITING DEPHOSPHORYLATION
The hydrolysis of 0-p-phenylazophenylphosphorothioate by Escherichia coli alkaline phosphatase was studied by the stopped-flow technique. “Burst” kinetics is observed at both acid and basic pH, suggesting that a step following thiophosphorylation is rate-limiting at all pH values. At pH 8.5, activation of a second active site on the enzyme dimer is observed in the transient phase as subsrrate c...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2013
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.27.1_supplement.lb194