Action Pattern of Serum Amylase Using p-Nitrophenyl-maltoheptaoside as Substrate
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چکیده
منابع مشابه
Automated measurement of amylase isoenzymes with 4-nitrophenyl-maltoheptaoside as substrate and use of a selective amylase inhibitor.
We automated a kinetic procedure for determining amylase isoenzymes in serum and urine samples. We used 4-nitro-phenylmaltoheptaoside as substrate and a selective amylase inhibitor with the Abbott-VP bichromatic system. By use of the maximum differences between pancreatic (P) and salivary (S) amylase activities remaining after inhibition by the selective inhibitor and by use of the linear range...
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Reference ranges for -amylase in serum, spontaneously voided urine, and 24h urine were determined, using 4,6-ethylidene-(G7)-l-4-nitrophenyl-(Gl)-a,£)-malthoheptaoside äs the Substrate (EPS method), at 25, 30, and 37 °C. The measured values were evaluated with and without the use of a factor which converts the results of the -amylase EPS method into values comparable to those obtained with the ...
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The effects of varying concentrations of sodium chloride and formaldehyde on the activity of “usual” and “atypical” serum cholinesterases using o-nitrophenyl butyrate as substrate have been examined. The atypical enzyme has been shown to be more sensitive to either inhibitor than the usual enzyme. These results indicate two new methods for differentiating the two variants using a noncholine est...
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Cytoplasmic aldehyde dehydrogenase catalyses the hydrolysis of methyl p-nitrophenyl (PNP) carbonate at an appreciable rate that is markedly stimualted by NAD+ or NADH. The nuleotides accelerate the rate-limiting hydrolysis of the acyl-enzyme intermediate while slowing the observed burst of p-nitrophenoxide production. With PNP dimethylcarbamate the enzyme catalyses the slow release of approx. 1...
متن کاملL-Phenylalanine inhibition of human alkaline phosphatases with p-nitrophenyl phosphate as substrate.
With p-nitrophenyl phosphate as the substrate, there reportedly is no organ-specific inhibition of alkaline phosphatase (EC 3.1.3.1) activity by L-phenylalanine. However, we found that at pH 10.0, with p-nitrophenyl phosphate as the substrate, L-phenylalanine obviously inhibits the alkaline phosphatase isoenzyme from human placenta, whereas there is little if any inhibition of the isoenzyme fro...
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ژورنال
عنوان ژورنال: Clinical Chemistry and Laboratory Medicine
سال: 1984
ISSN: 1434-6621,1437-4331
DOI: 10.1515/cclm.1984.22.6.427