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Literature DB >> 6161115

A simultaneous-coupling azo dye method for the quantitative assay of esterase using alpha-naphthyl acetate as substrate.

Abstract

This paper describes a simultaneous-coupling azo dye method for the measurement of esterase activity using the histochemical substrate, alpha-naphthyl acetate. By the choice of two diazonium salts with optimal coupling characteristics, the reaction can be carried out at any pH between 3.0 and 9.5. The azo dye is maintained in solution for spectrophotometric measurements with bovine serum albumin. The simultaneous-coupling method is compared with an assay based on the direct measurement of released alpha-naphthol by its ultra-violet absorbance in a pH study of hog liver esterase. There is good agreement between the data obtained by both methods.

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Year: 1980 PMID： 6161115 DOI： 10.1007/BF01024552

Source DB: PubMed Journal: Histochem J ISSN： 0018-2214

8 in total

1. QUANTITATIVE CHARACTERIZATION OF A HISTOCHEMICAL ENZYME SYSTEM.

Authors: V K HOPSU; P J MCMILLAN
Journal: J Histochem Cytochem Date: 1964-05 Impact factor: 2.479

2. Protein binding of azo dyes by tissue homogenates.

Authors: A M RUTENBURG; A M SELIGMAN
Journal: J Histochem Cytochem Date: 1956-01 Impact factor: 2.479

3. Human esterases.

Authors: G GOMORI
Journal: J Lab Clin Med Date: 1953-09

4. The colorimetric determination of lipase and esterase in human serum.

Authors: A M SELIGMAN; M M NACHLAS
Journal: J Clin Invest Date: 1950-01 Impact factor: 14.808

5. A biochemical study of non-specific esterases from plant cells, employing the histochemical substrate, naphthol AS-D acetate.

Authors: D J James; A R Smith
Journal: Histochem J Date: 1974-01

6. A quantitative histochemical technique for the estimation of azo dye coupling reactions.

Authors: A Jarrett; N W Please
Journal: Histochem J Date: 1970-07

7. A new and simple procedure for serum arylesterase.

Authors: A Burline; L Galzigna
Journal: Clin Chim Acta Date: 1972-06 Impact factor: 3.786

8. A histochemical enzyme kinetic system applied to the trypsin-like amidase and esterase activity in human mast cells.

Authors: V K HOPSU; G G GLENNER
Journal: J Cell Biol Date: 1963-06 Impact factor: 10.539

8 in total

5 in total

A simultaneous-coupling azo dye method for the quantitative assay of esterase using alpha-naphthyl acetate as substrate.

1. QUANTITATIVE CHARACTERIZATION OF A HISTOCHEMICAL ENZYME SYSTEM.

2. Protein binding of azo dyes by tissue homogenates.

3. Human esterases.

4. The colorimetric determination of lipase and esterase in human serum.

5. A biochemical study of non-specific esterases from plant cells, employing the histochemical substrate, naphthol AS-D acetate.

6. A quantitative histochemical technique for the estimation of azo dye coupling reactions.

7. A new and simple procedure for serum arylesterase.

8. A histochemical enzyme kinetic system applied to the trypsin-like amidase and esterase activity in human mast cells.

1. Carboxylic ester hydrolases in mitochondria from rat skeletal muscle.

Review 2. The histochemistry of carboxylester hydrolases: problems and possibilities.

3. Identification of aspirinase with one of the carboxylesterases requiring a thiol group.

4. [3H]Indole-3-acetyl-myo-inositol hydrolysis by extracts of Zea mays L. vegetative tissue.

5. Fast Blue RR-Siloxane Derivatized Materials Indicate Wound Infection Due to a Deep Blue Color Development.