US3703441A - Diagnostic reagents for the determination of gamma-glutamyl transpeptidase in human serum - Google Patents

Diagnostic reagents for the determination of gamma-glutamyl transpeptidase in human serum Download PDF

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Publication number
US3703441A
US3703441A US47141A US3703441DA US3703441A US 3703441 A US3703441 A US 3703441A US 47141 A US47141 A US 47141A US 3703441D A US3703441D A US 3703441DA US 3703441 A US3703441 A US 3703441A
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solution
surface active
determination
active agents
buffer solution
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US47141A
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Kazuo Nakanishi
Shuzo Takei
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Sankyo Co Ltd
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Sankyo Co Ltd
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    • G—PHYSICS
    • G10—MUSICAL INSTRUMENTS; ACOUSTICS
    • G10H—ELECTROPHONIC MUSICAL INSTRUMENTS; INSTRUMENTS IN WHICH THE TONES ARE GENERATED BY ELECTROMECHANICAL MEANS OR ELECTRONIC GENERATORS, OR IN WHICH THE TONES ARE SYNTHESISED FROM A DATA STORE
    • G10H1/00—Details of electrophonic musical instruments
    • G10H1/02—Means for controlling the tone frequencies, e.g. attack or decay; Means for producing special musical effects, e.g. vibratos or glissandos
    • G10H1/04—Means for controlling the tone frequencies, e.g. attack or decay; Means for producing special musical effects, e.g. vibratos or glissandos by additional modulation
    • G10H1/053—Means for controlling the tone frequencies, e.g. attack or decay; Means for producing special musical effects, e.g. vibratos or glissandos by additional modulation during execution only
    • G10H1/055—Means for controlling the tone frequencies, e.g. attack or decay; Means for producing special musical effects, e.g. vibratos or glissandos by additional modulation during execution only by switches with variable impedance elements
    • G10H1/0555—Means for controlling the tone frequencies, e.g. attack or decay; Means for producing special musical effects, e.g. vibratos or glissandos by additional modulation during execution only by switches with variable impedance elements using magnetic or electromagnetic means
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/48—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving transferase

Definitions

  • This invention relates to a diagnostic reagent. More particularly, it is concerned with a diagnostic reagent for the detection and quantitative determination of 'y-glutamyl transpeptidase (hereinafter referred to as 'y-G'IPase) in human serum which comprises a specific combination of 'y-L-glutamic acid p-nitroanilide, a selected surface active agent and a selected buffer solution.
  • 'y-G'IPase 'y-glutamyl transpeptidase
  • liver diseases e.g. cancer of liver, obstructive liver diseases and the like.
  • a 'y-GNA solution which is stable at a high concentration and is useful as a diagnostic reagent, can be obtained by selecting and employing a particular combination of 'y-GNA with a specific surface active agent and a specific buffer solution.
  • a primary object of this invention to provide a highly stable and high substrate concentration diagnostic reagent for the determination of 'y-GTPase in human serum which comprises a combination of 'y-GNA and a particular amphoteric or non-ionic surface active agent and a particular buffer solution.
  • the diagnostic reagent of this invention has been completed based upon the above finding and, in particular, comprises a novel combination of (2) one or more surface active agents selected from the group consisting of amphoteric surface active agents and non-ionic surface active agents, and
  • a buffer solution selected from the group consisting of a collidine buffer solution, a boric acid buffer solution, a 5,5-diethylbarbituric acid buffer solution and an ammonia buifer solution.
  • a conventional solvent for example, an alcohol, e.g. methanol, ethanol, propanol, butanol, glycerol and the like; a ketone, e.g. acetone, methyl ethyl ketone, and the like; a lower aliphatic acid ester, e.g. ethyl acetate, butyl acetate and the like; a heterocyclic base, e.g. pyridine, quinoline and the like; an aromatic hydrocarbon, e.g.
  • the substrate solution of a high concentration above approximately 5 mM. could be provided.
  • the following surface active agents were tested: For instance, cationic surface active agents such as those containing quarternary ammonium ions, e.g. benzethonium chloride, benzalkonium chloride and the like; anionic surface active agents such as those containing derivatives of carboxylic, sulfonic or sulfuric acids, e.g. sodium laurate, sodium dodecylbenzenesulfonate, sodium alcohol polyethenoxy sulfate; amphoteric surface active agents such as those containing imidazoline compounds, e.g.
  • Miranol or N-acyl sarcosine, e.g. sodium N-lauroylsarcosine; as well as nonionic surface active agents such as those containing a mixed ether of an alcohol and a phenol, e.g. polyoxyethylene nonyl phenol ether, polyoxyethylene octyl alcohol ether.
  • N-acyl sarcosine e.g. sodium N-lauroylsarcosine
  • nonionic surface active agents such as those containing a mixed ether of an alcohol and a phenol, e.g. polyoxyethylene nonyl phenol ether, polyoxyethylene octyl alcohol ether.
  • reaction employed for accomplishment of the purpose of this invention is an enzymatic reaction and thus one should, of course, select such a surface active agent that could not inhibit this reaction.
  • amphoteric and non-ionic surface active agents do not in any way inhibit the 'y-GTPaSe activity, whereas cationic and anionic surface active agents remarkably inhibit said activity.
  • Nikkol. NE s 202 trade name, available from Nikko Chemicals Co., Ltd., Japan.
  • Nikkol Sarcosinate LN, trade name, available from Nikko Chemicals Co., Ltd., Japan.
  • Nilrkol N P-9 trade name, available from Nikko Chemicals Co.
  • b l i cil BO 20 trade name, available from Nikko Chemicals Co., Ltd., Japan.
  • a solution of g. of one of the above-listed surface active agents, 150 mg. of 'y-GNA and 396 mg. of glycylglycine in about 90 ml. of distilled Water is adjusted to pH 8 with addition of hydrochloric acid or an aqueous solution of sodium hydroxide and made up the whole amount to 100 ml. with addition of a suitable amount of distilled water.
  • the resulting solution is employed as a substrate solution.
  • the mixture of 0.5 ml. of the substrate solution with 0.01 ml. of serum is allowed to stand at 37 C. for 30 minutes and then 2.5 ml. of an 1.3 M aqueous acetic acid solution is added thereto.
  • the absorbance at 410 mp. is measured in a conventional manner.
  • the substrate, 7-GNA which can be employed in this invention shows extremely diiferent stabilities in the same pH range, depending upon the kinds and types of the buffer solutions employed and that this substrate is very unstable in the tris buffer solution previously utilized for the determination of the -GTPase activity and various phosphate buffer solutions with a wide pH range from weakly acidic to weakly basic which are commonly utilized in an enzymatic reaction.
  • the same substrate solution in the above Table I is employed except that Nikkol NP-9 is employed as a surface active agent and the indicated buffer solution of pH 8.0 is employed instead of the distilled water and the acid or base.
  • the absorbance at AE was measured. The difference obtained by deducting the former measured value from the latter one is defined as the stability value.
  • the final concentration of the surface active agent employed in this invention is desirably within the range of about 2.5 to 15% in the reagent for the determination of 'y-GTPase, with about 5% being most preferable.
  • the ionic strength of the buifer solution employed in the present reagent may be widely varied mainly depending upon the kinds and types of the buffer solutions employed, but the preferable strength is within the range of about 0.05 to 0.3, with about 0.1 for the collidine or ammonia buffer solution, about 0.2 to 0.3 for the boric acid buffer solution and less than about 0.1 for the Veronal buffer solution being most preferable.
  • reaction rate may be accomplished, not essential, by further addition to the present reagent of a suitable amount of a peptide derivative having free terminal amino groups such as glycylglycine and the like as an acceptor for the 'y-glutamic acid which may be produced in situ as a consequence of an enzymatic reaction.
  • a suitable amount of a peptide derivative having free terminal amino groups such as glycylglycine and the like as an acceptor for the 'y-glutamic acid which may be produced in situ as a consequence of an enzymatic reaction.
  • the procedure for determining 'y-GTPase in human serum may be favourably carried out by a slight modification of the well-known determination method, for example, that disclosed by D. M. Dimov et al. in Clinica Chemica Acta, 16, 271 (1967). The details of the determination procedure will be set forth hereinbelow, the disclosure of which is incorporated herein as a reference.
  • a mixture of 0.5 ml. of the reagent with 0.02 ml. of human serum is allowed to stand at 37 C. for minutes and then 2.5 H11. of a 1.3 M aqueous acetic acid solution is added thereto.
  • the absorbance at 410 m is measured in a conventional manner.
  • 0.5 ml. of the reagent is allowed to stand at 37 C. for 30 minutes and then 2.5 ml. of a 1.3 M aqueous acetic acid solution and 0.02 ml. of serum are added thereto.
  • the absorbance at 410 m is also measured as above.
  • the difference obtained by deducting the latter measured value from the former one is defined as the activity value.
  • the diagnostic reagent was prepared having the following composition:
  • the reagent was prepared as follows.
  • the 'y-GNA was dissolved in the hydrochloric acid (referred to as Solution A).
  • the glycylglycine and the Nikkol were dissolved in a portion of about 55 ml. of the distilled water and then the resulting solution adjusted to pH 8.0 by addition of dilute aqueous sodium hydroxide to form an alkaline solution (referred to as Solution B).
  • Solution B dilute aqueous sodium hydroxide
  • To the Solution B were added the Solution A and the Veronal buffer solution and then a sufiicient amount of distilled water was added thereto to make up the whole volume to 100 ml.
  • EXAMPLE 2 The diagnostic reagent was prepared having the same composition as in the above Example 1 except that g. of Nikkol NP-9 was employed instead of the 5 g. and 30 ml. of /s M collidine-hydrochloric acid (pH 8.0) bufier solution was employed instead of the Veronal buffer solution.
  • EXAMPLE 3 The diagnostic reagent was prepared having the same composition as in the above Example 1 except that 2.5 g. of Nikkol NP-9 was employed instead of the 5 g. and 15.5 ml. of a ,5 N aqueous ammonia was employed instead of the Veronal buffer solution.
  • EXAMPLE 4 The diagnostic reagent was prepared having the same composition as in above Example 1 except that 18.3 ml. of /5 M boric acid-sodium carbonate buffer solution (pH 8.0) was employed instead of the Veronal buffer solution.
  • EXAMPLE 5 The diagnostic reagent was prepared having the same composition as in the above Example 1 except that 5 g. of
  • Nikkol BO 20 was employed instead of the Nikkol NP-9.
  • EXAMPLE 6 The diagnostic reagent was prepared having the same composition as in the above Example 1 except that 5 g. of Miranol C2M-SF was employed instead of the Nikkol NP-9.
  • EXAMPLE 7 The diagnostic reagent was prepared having the same composition as in the above Example 1 except that 5 g. of Miranol C2M-SF was employed instead of the Nikkol NP9 and 15.5 ml. of ,5 N aqueous ammonia was employed instead of the Veronal buffer solution.
  • a diagnostic reagent for the determination of 'yglutamyl transpeptidase in human serum which comprises a combination of (1) 'y-glutamic acid p-nitroanilide,
  • one or more surface active agents selected from the group consisting of an N-acyl sarcosine, an imidazoline amphoteric compound, a polyoxyethylene alcohol ether and a polyoxyethylene phenol ether, and
  • a buffer solution selected from the group consisting of a collidine buffer solution, a boric acid bufier solution, a 5,5-diethylbarbituric acid buifer solution and an ammonia buffer solution.
  • said surface active agent is that containing sodium lauroylsarcosine, an imidazoline, polyoxyethylene nonyl phenol ether or polyoxyethylene octyl alcohol ether.
  • the reagent according to claim 1 wherein said bufier solution is a collidine-hydrochloric acid buffer solution, a boric acid-sodium carbonate buffer solution, a sodium 5,S-diethylbarbiturate-sodium acetate buffer solution or aqueous ammonia.

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  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
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  • Physics & Mathematics (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
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US47141A 1969-06-23 1970-06-17 Diagnostic reagents for the determination of gamma-glutamyl transpeptidase in human serum Expired - Lifetime US3703441A (en)

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JP44049592A JPS4910718B1 (enrdf_load_stackoverflow) 1969-06-23 1969-06-23

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JP (1) JPS4910718B1 (enrdf_load_stackoverflow)
DE (1) DE2032270A1 (enrdf_load_stackoverflow)
FR (1) FR2071603A5 (enrdf_load_stackoverflow)
GB (1) GB1312668A (enrdf_load_stackoverflow)

Cited By (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3769173A (en) * 1972-08-21 1973-10-30 Warner Lambert Co Determination of gamma-glutamyl transpeptidase in biological fluids
US3986931A (en) * 1972-12-05 1976-10-19 Boehringer Mannheim G.M.B.H. γ-GLUTAMYL-4-NITROANILIDE COMPOUNDS AND THEIR USE IN DETERMINING γ-GLUTAMYL TRANSPEPTIDASE
US4049702A (en) * 1972-12-05 1977-09-20 Boehringer Mannheim G.M.B.H. γ-Glutamyl-4-nitroanilide compounds
US4425427A (en) 1980-03-13 1984-01-10 Vitafin N.V. Simultaneous, kinetic, spectrophotometric analysis of blood serum for multiple components
US4448715A (en) * 1981-11-02 1984-05-15 University Of Miami Tagged pyroglu-L-Phe-L-Arg derivatives, substrates and assays for kallikrein
WO1984004931A1 (en) * 1983-06-08 1984-12-20 Coulter Electronics Method and composition for determination of gamma glutamyl transpeptidase
US4511651A (en) * 1982-07-30 1985-04-16 American Monitor Corporation Reagent composition and assay for the determination of γ-glutamyltransferase activity
US4751178A (en) * 1985-09-26 1988-06-14 Eastman Kodak Company Substrates, compositions, elements and methods for the determination of gamma-glutamyltransferase

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE2917999A1 (de) * 1979-05-04 1980-11-13 Behringwerke Ag Substrat zur bestimmung der gama -glutamyltranspeptidase

Cited By (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3769173A (en) * 1972-08-21 1973-10-30 Warner Lambert Co Determination of gamma-glutamyl transpeptidase in biological fluids
US3986931A (en) * 1972-12-05 1976-10-19 Boehringer Mannheim G.M.B.H. γ-GLUTAMYL-4-NITROANILIDE COMPOUNDS AND THEIR USE IN DETERMINING γ-GLUTAMYL TRANSPEPTIDASE
US4049702A (en) * 1972-12-05 1977-09-20 Boehringer Mannheim G.M.B.H. γ-Glutamyl-4-nitroanilide compounds
US4425427A (en) 1980-03-13 1984-01-10 Vitafin N.V. Simultaneous, kinetic, spectrophotometric analysis of blood serum for multiple components
US4448715A (en) * 1981-11-02 1984-05-15 University Of Miami Tagged pyroglu-L-Phe-L-Arg derivatives, substrates and assays for kallikrein
US4511651A (en) * 1982-07-30 1985-04-16 American Monitor Corporation Reagent composition and assay for the determination of γ-glutamyltransferase activity
WO1984004931A1 (en) * 1983-06-08 1984-12-20 Coulter Electronics Method and composition for determination of gamma glutamyl transpeptidase
US4560650A (en) * 1983-06-08 1985-12-24 Coulter Electronics, Inc. Method and compositions for determination of gamma glutamyl transpeptidase
US4751178A (en) * 1985-09-26 1988-06-14 Eastman Kodak Company Substrates, compositions, elements and methods for the determination of gamma-glutamyltransferase

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JPS4910718B1 (enrdf_load_stackoverflow) 1974-03-12
FR2071603A5 (enrdf_load_stackoverflow) 1971-09-17
DE2032270A1 (de) 1970-12-23
GB1312668A (en) 1973-04-04

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