CA2368007A1 - Composition for patient sample preparation - Google Patents
Composition for patient sample preparation Download PDFInfo
- Publication number
- CA2368007A1 CA2368007A1 CA002368007A CA2368007A CA2368007A1 CA 2368007 A1 CA2368007 A1 CA 2368007A1 CA 002368007 A CA002368007 A CA 002368007A CA 2368007 A CA2368007 A CA 2368007A CA 2368007 A1 CA2368007 A1 CA 2368007A1
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- CA
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- Prior art keywords
- composition
- amino
- salt
- mixtures
- group
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
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- 239000000203 mixture Substances 0.000 title claims abstract description 38
- 239000013610 patient sample Substances 0.000 title claims abstract description 8
- 238000002360 preparation method Methods 0.000 title description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 claims abstract description 29
- 239000000872 buffer Substances 0.000 claims abstract description 16
- 150000001413 amino acids Chemical class 0.000 claims abstract description 13
- UXFQFBNBSPQBJW-UHFFFAOYSA-N 2-amino-2-methylpropane-1,3-diol Chemical compound OCC(N)(C)CO UXFQFBNBSPQBJW-UHFFFAOYSA-N 0.000 claims abstract description 12
- 239000003599 detergent Substances 0.000 claims abstract description 12
- 150000003839 salts Chemical class 0.000 claims abstract description 12
- 230000002378 acidificating effect Effects 0.000 claims abstract description 5
- 239000006163 transport media Substances 0.000 claims abstract description 5
- 238000000034 method Methods 0.000 claims abstract description 3
- 238000012545 processing Methods 0.000 claims abstract description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 14
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 claims description 9
- 239000004471 Glycine Substances 0.000 claims description 7
- 210000002966 serum Anatomy 0.000 claims description 7
- 229920004890 Triton X-100 Polymers 0.000 claims description 6
- 239000013504 Triton X-100 Substances 0.000 claims description 6
- 239000004475 Arginine Substances 0.000 claims description 3
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims description 3
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 3
- 239000004472 Lysine Substances 0.000 claims description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 3
- 229920002114 octoxynol-9 Polymers 0.000 claims description 3
- 159000000000 sodium salts Chemical class 0.000 claims description 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 2
- XAEFZNCEHLXOMS-UHFFFAOYSA-M potassium benzoate Chemical compound [K+].[O-]C(=O)C1=CC=CC=C1 XAEFZNCEHLXOMS-UHFFFAOYSA-M 0.000 claims 2
- 239000000427 antigen Substances 0.000 abstract description 7
- 102000036639 antigens Human genes 0.000 abstract description 7
- 108091007433 antigens Proteins 0.000 abstract description 7
- 239000000523 sample Substances 0.000 abstract description 7
- 239000002253 acid Substances 0.000 abstract description 4
- RPAJSBKBKSSMLJ-DFWYDOINSA-N (2s)-2-aminopentanedioic acid;hydrochloride Chemical class Cl.OC(=O)[C@@H](N)CCC(O)=O RPAJSBKBKSSMLJ-DFWYDOINSA-N 0.000 abstract description 3
- 238000001514 detection method Methods 0.000 abstract description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 238000003556 assay Methods 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 6
- 238000003018 immunoassay Methods 0.000 description 6
- 239000007983 Tris buffer Substances 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 238000011161 development Methods 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 230000000694 effects Effects 0.000 description 3
- 230000009871 nonspecific binding Effects 0.000 description 3
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 230000027455 binding Effects 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 201000006747 infectious mononucleosis Diseases 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 238000006386 neutralization reaction Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 1
- 241001505901 Streptococcus sp. 'group A' Species 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 230000000845 anti-microbial effect Effects 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000012888 bovine serum Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000013020 final formulation Substances 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- WSFSSNUMVMOOMR-NJFSPNSNSA-N methanone Chemical compound O=[14CH2] WSFSSNUMVMOOMR-NJFSPNSNSA-N 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 230000003071 parasitic effect Effects 0.000 description 1
- -1 polyoxyethylenes Polymers 0.000 description 1
- 235000011164 potassium chloride Nutrition 0.000 description 1
- 239000001103 potassium chloride Substances 0.000 description 1
- 159000000001 potassium salts Chemical class 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 239000012898 sample dilution Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/5306—Improving reaction conditions, e.g. reduction of non-specific binding, promotion of specific binding
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Analytical Chemistry (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Food Science & Technology (AREA)
- Medicinal Chemistry (AREA)
- Physics & Mathematics (AREA)
- Cell Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Peptides Or Proteins (AREA)
Abstract
The object of the present invention is to claim a composition which when add ed to a patient sample containing a target antigen in an acidic or formalin- containing transport medium neutralizes the acid and formalin while preservi ng immunoreactivity of the antigen allowing its detection. The composition comprises an amino glycol buffer, an amino acid, a salt, and a non-ionic detergent. A further object of the present invention is to claim a method of processing a sample by adding a composition comprising an amino glycol buffe r, an amino acid, a salt, and a non-ionic detergent.
Description
COMPOSITION FOR PATIENT SAMPLE PREPARATION
Background of the Invention Enteric stool specimens are frequently collected in a 10% formalin or sodium acetate-acetic acid-formalin (SAF) transport medium which serves to 1 o inactivate the infectivity and preserve the morphology of parasitic organisms in the sample. These media may have adverse effects on the function of antibodies in diagnostic immunoassays.
Formalin, also known as formaldehyde, binds to amino groups on proteins, potentially altering their structure and functional activity. Low pH, 15 such as from the acetic acid in SAF, is inhibitory to antigen-antibody binding.
The development of an effective diagnostic immunoassay for enteric stool specimens collected in formalin or SAF, therefore, depends on the ability to counteract these adverse effects. Although some microwell and flow-through enzyme immunoassays appear to accomplish this through sample dilution, 2o simpler and more effective approaches are needed.
Summary of the Invention The object of the present invention is to claim a composition which when added to a patient sample containing a target antigen in an acidic or formalin-containing transport medium neutralizes the acid and formalin while preserving 2s immunoreactivity of the antigen allowing its detection. The composition comprises an amino glycol buffer, an amino acid, a salt, and a non-ionic detergent.
A further object of the present invention is to claim a method of processing a sample by adding a composition comprising an amino glycol buffer, 3o an amino acid, a salt, and a non-ionic detergent.
Detailed Description of the Invention The present invention is based on the discovery that a composition comprising an amino glycol buffer, an amino acid, a salt, and a non-ionic detergent can, when added to a patient sample containing a target antigen in an acidic or formalin-containing transport medium, allow for the neutralization of the acid and formalin while preserving immunoreactivity of the antigen allowing its detection.
The composition of the present invention includes an amino glycol buffer.
Suitable amino gylcol buffers include 2-amino-2hydroxymethyl-1,3-propanediol to (Tris buffer), 2-amino-2-methyl-1,3-propanediol.
The present composition further includes an amino acid. Suitable amino acids include glycine, lysine and arginine.
The composition further includes a salt. Suitable salts include sodium salts such as sodium chloride and potassium salts such as 1s potassium chloride.
The composition of the present invention further includes a non-ionic detergent. Suitable non-ionic detergents include polyoxyethylenes such as t-octylphenoxypolyethoxyethanol (Triton X-100) and (octylphenoxyl)-polyethoxyethanol (Nonidet P-40).
2o The composition of the present invention may further include serum. It is believed that serum serves to prevent or reduce non-specific binding of antibodies that may be subsequently used in an immunoassay when non-specific binding is a problem. Suitable serums include normal mammalian serum of any kind, such as that derived from humans. Other mammalian serums include 2s bovine, porcine, equine and murine.
Formulation:
The key elements of the treatment buffer formulation are the use of an amino acid in a basic buffer medium. We have selected glycine as the amino acid, and Tris base as the basic buffer . Also included in the treatment buffer is 3o some detergent, Triton X-100, which appears to help extract antigens relevant to our specific assay from the stool matrix, sodium chloride to help mimic physiological salt conditions which are theoretically ideal for antigen-antibody binding to occur, and sodium azide, which is added as an anti-microbial preservative. In addition, normal bovine serum was added to block non-specific binding.
The final formulation consists of 1 M Tris, 1 M glycine, 0.9% sodium chloride, 0.5% Triton X-100, and 0.01% sodium azide. The sources of the chemicals we have used to develop the treatment buffer are the Sigma Chemical to Company (St. Louis, Mo USA) and the J.T. Baker Chemical Company (Phillipsburg, NJ USA). The vendor catalog numbers are: Tris Base (also known as Trizma Base), Sigma T-1503; Glycine, Sigma G-7126; Sodium chloride, Baker 3624-07; Triton X-100, Sigma T-6878; and Sodium azide, Sigma S-2002. These chemicals are standard grade materials and we have no reason to believe that is other sources of these chemicals would not be equally as effective.
Eff~:
The need for a treatment buffer became apparent during our early development work on lateral flow immunoassays where a stool specimens was the patient sample being tested. It was noted that 10% formalin or SAF when 2o run directly in our lateral flow assays severely weakened or completely eliminated the development of test and control lines.
Therefore, tests were run in an attempt to eliminate the interference caused by formalin using a Group A Streptococcus assay (Rapid Strep A test, Genzyme Diagnostics, San Carlos, California) and an Infectious Mononucleosis 25 assay (Rapid Mono test, Genzyme Diagnostics), both lateral flow assays. We discovered that formalin or SAF did not cause an antibody-specific inhibition of signal, but was a more generalized phenomenon that would be applicable to many different immunoassays of this type.
Initially, after demonstrating that adding various types of carrier proteins 3o was relatively ineffective in counteracting formalin, glycine was tried and shown to be effective. However when SAF-treated stool samples were tested, significant inhibitory effects on signal were still observed. It appears that this inhibition was caused by the presence of acetic acid, which made the samples rather acidic in pH. When Tris base was added to such samples, signal was restored.
The data shown in the table below illustrates the suppressive effects of SAF on control line signal development in a lateral flow assay. These assays utilize goat anti-mouse IgG antibody striped onto a membrane, which in turn to captures a particulate-labeled mouse IgG antibody to generate a visible signal.
As shown, the use of the sample treatment buffer (STB) restores the control line signal to approximately the same intensity as the control level.
Table Sample Device Control Line Intensity Control (water) ++++
Without STB (SAF + water) -With STB (SAF + STB ++++
In the above experiments, no formal incubation time was used. The treatment buffer was added immediately prior to pipeting the sample into the test devices.
The chemical reactions, which neutralize formalin and acid occur quickly and functionally, can be thought of as instantaneous. It is possible that additional 2o neutralization may take place as the sample is flowing in the device.
Background of the Invention Enteric stool specimens are frequently collected in a 10% formalin or sodium acetate-acetic acid-formalin (SAF) transport medium which serves to 1 o inactivate the infectivity and preserve the morphology of parasitic organisms in the sample. These media may have adverse effects on the function of antibodies in diagnostic immunoassays.
Formalin, also known as formaldehyde, binds to amino groups on proteins, potentially altering their structure and functional activity. Low pH, 15 such as from the acetic acid in SAF, is inhibitory to antigen-antibody binding.
The development of an effective diagnostic immunoassay for enteric stool specimens collected in formalin or SAF, therefore, depends on the ability to counteract these adverse effects. Although some microwell and flow-through enzyme immunoassays appear to accomplish this through sample dilution, 2o simpler and more effective approaches are needed.
Summary of the Invention The object of the present invention is to claim a composition which when added to a patient sample containing a target antigen in an acidic or formalin-containing transport medium neutralizes the acid and formalin while preserving 2s immunoreactivity of the antigen allowing its detection. The composition comprises an amino glycol buffer, an amino acid, a salt, and a non-ionic detergent.
A further object of the present invention is to claim a method of processing a sample by adding a composition comprising an amino glycol buffer, 3o an amino acid, a salt, and a non-ionic detergent.
Detailed Description of the Invention The present invention is based on the discovery that a composition comprising an amino glycol buffer, an amino acid, a salt, and a non-ionic detergent can, when added to a patient sample containing a target antigen in an acidic or formalin-containing transport medium, allow for the neutralization of the acid and formalin while preserving immunoreactivity of the antigen allowing its detection.
The composition of the present invention includes an amino glycol buffer.
Suitable amino gylcol buffers include 2-amino-2hydroxymethyl-1,3-propanediol to (Tris buffer), 2-amino-2-methyl-1,3-propanediol.
The present composition further includes an amino acid. Suitable amino acids include glycine, lysine and arginine.
The composition further includes a salt. Suitable salts include sodium salts such as sodium chloride and potassium salts such as 1s potassium chloride.
The composition of the present invention further includes a non-ionic detergent. Suitable non-ionic detergents include polyoxyethylenes such as t-octylphenoxypolyethoxyethanol (Triton X-100) and (octylphenoxyl)-polyethoxyethanol (Nonidet P-40).
2o The composition of the present invention may further include serum. It is believed that serum serves to prevent or reduce non-specific binding of antibodies that may be subsequently used in an immunoassay when non-specific binding is a problem. Suitable serums include normal mammalian serum of any kind, such as that derived from humans. Other mammalian serums include 2s bovine, porcine, equine and murine.
Formulation:
The key elements of the treatment buffer formulation are the use of an amino acid in a basic buffer medium. We have selected glycine as the amino acid, and Tris base as the basic buffer . Also included in the treatment buffer is 3o some detergent, Triton X-100, which appears to help extract antigens relevant to our specific assay from the stool matrix, sodium chloride to help mimic physiological salt conditions which are theoretically ideal for antigen-antibody binding to occur, and sodium azide, which is added as an anti-microbial preservative. In addition, normal bovine serum was added to block non-specific binding.
The final formulation consists of 1 M Tris, 1 M glycine, 0.9% sodium chloride, 0.5% Triton X-100, and 0.01% sodium azide. The sources of the chemicals we have used to develop the treatment buffer are the Sigma Chemical to Company (St. Louis, Mo USA) and the J.T. Baker Chemical Company (Phillipsburg, NJ USA). The vendor catalog numbers are: Tris Base (also known as Trizma Base), Sigma T-1503; Glycine, Sigma G-7126; Sodium chloride, Baker 3624-07; Triton X-100, Sigma T-6878; and Sodium azide, Sigma S-2002. These chemicals are standard grade materials and we have no reason to believe that is other sources of these chemicals would not be equally as effective.
Eff~:
The need for a treatment buffer became apparent during our early development work on lateral flow immunoassays where a stool specimens was the patient sample being tested. It was noted that 10% formalin or SAF when 2o run directly in our lateral flow assays severely weakened or completely eliminated the development of test and control lines.
Therefore, tests were run in an attempt to eliminate the interference caused by formalin using a Group A Streptococcus assay (Rapid Strep A test, Genzyme Diagnostics, San Carlos, California) and an Infectious Mononucleosis 25 assay (Rapid Mono test, Genzyme Diagnostics), both lateral flow assays. We discovered that formalin or SAF did not cause an antibody-specific inhibition of signal, but was a more generalized phenomenon that would be applicable to many different immunoassays of this type.
Initially, after demonstrating that adding various types of carrier proteins 3o was relatively ineffective in counteracting formalin, glycine was tried and shown to be effective. However when SAF-treated stool samples were tested, significant inhibitory effects on signal were still observed. It appears that this inhibition was caused by the presence of acetic acid, which made the samples rather acidic in pH. When Tris base was added to such samples, signal was restored.
The data shown in the table below illustrates the suppressive effects of SAF on control line signal development in a lateral flow assay. These assays utilize goat anti-mouse IgG antibody striped onto a membrane, which in turn to captures a particulate-labeled mouse IgG antibody to generate a visible signal.
As shown, the use of the sample treatment buffer (STB) restores the control line signal to approximately the same intensity as the control level.
Table Sample Device Control Line Intensity Control (water) ++++
Without STB (SAF + water) -With STB (SAF + STB ++++
In the above experiments, no formal incubation time was used. The treatment buffer was added immediately prior to pipeting the sample into the test devices.
The chemical reactions, which neutralize formalin and acid occur quickly and functionally, can be thought of as instantaneous. It is possible that additional 2o neutralization may take place as the sample is flowing in the device.
Claims (12)
1. A composition comprising an amino glycol buffer, an amino acid, a salt and a non-ionic detergent.
2. The composition of claim 1, wherein the amino glycol is selected from the group consisting of 2-amino-2hydroxymethyl-1,3-propanediol, 2-amino-2-methyl-1,3-propanediol, and mixtures thereof.
3. The composition of claim 1, wherein the amino acid is selected from the group consisting of glycine, lysine, arginine, and mixtures thereof.
4. The composition of claim 1, wherein the salt is selected from the group consisting of sodium salt, potassium salt, and mixtures thereof.
5. The composition of claim 1, wherein the non-ionic detergent is selected from the group consisting of t-octylphenoxypolyethoxyethanol (Triton X-100)(octylphenoxyl)-polyethoxyethanol (Nonidet P-40), and mixtures thereof.
6. The composition of claim 1, the composition further comprising a serum.
7. A method of processing a patient sample comprising the steps of:
(a) obtaining the patient sample containing a formaldehyde or an acidic transport medium;
(b) adding a composition comprising an amino glycol buffer, an amino acid, a salt and a non-ionic detergent.
(a) obtaining the patient sample containing a formaldehyde or an acidic transport medium;
(b) adding a composition comprising an amino glycol buffer, an amino acid, a salt and a non-ionic detergent.
8. The composition of claim 7, wherein the amino gycol is selected from the group consisting of 2-amino-2hydroxymethyl-1,3-propanediol, 2-amino-2-methyl-1,3-propanediol, and mixtures thereof.
9. The composition of claim 7, wherein the amino acid is selected from the group consisting of glycine, lysine, arginine and mixtures thereof.
10. The composition of claim 7, wherein the salt is selected from the group consisting of sodium salt, potassium salt, and mixtures thereof.
11. The composition of claim 7, wherein the non-ionic detergent is selected from the group consisting of t-octylphenoxypolyethoxyethanol (Triton X-100), (octylphenoxyl)-polyethoxyethanol (Nonidet P-40) and mixtures thereof.
12. The composition of claim 7, the composition further comprising a serum.
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| PCT/US1999/007573 WO2000060353A1 (en) | 1999-04-06 | 1999-04-06 | Composition for patient sample preparation |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2368007A1 true CA2368007A1 (en) | 2000-10-12 |
Family
ID=22272513
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002368007A Abandoned CA2368007A1 (en) | 1999-04-06 | 1999-04-06 | Composition for patient sample preparation |
Country Status (5)
| Country | Link |
|---|---|
| EP (1) | EP1166111A1 (en) |
| JP (1) | JP2002541456A (en) |
| AU (1) | AU3475299A (en) |
| CA (1) | CA2368007A1 (en) |
| WO (1) | WO2000060353A1 (en) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE602007008728D1 (en) * | 2006-06-19 | 2010-10-07 | Becton Dickinson Co | PROCESSES AND COMPOSITIONS FOR THE CONSERVATION OF AMPLIFIED TISSUES, CELLS OR VIRUSES |
| US10190152B2 (en) | 2009-09-03 | 2019-01-29 | Becton, Dickinson And Company | Methods and compositions for direct chemical lysis |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5185264A (en) * | 1990-11-09 | 1993-02-09 | Abbott Laboratories | Diluent buffer and method for diluting an assay component |
| JPH06284886A (en) * | 1993-04-01 | 1994-10-11 | Amano Pharmaceut Co Ltd | Stabilization of enzyme in solution |
| US5695928A (en) * | 1993-12-10 | 1997-12-09 | Novartis Corporation | Rapid immunoassay for detection of antibodies or antigens incorporating simultaneous sample extraction and immunogenic reaction |
| US5958300A (en) * | 1998-02-06 | 1999-09-28 | Genzyme Corporation | Composition for patient sample preparation |
-
1999
- 1999-04-06 AU AU34752/99A patent/AU3475299A/en not_active Abandoned
- 1999-04-06 EP EP99916432A patent/EP1166111A1/en not_active Withdrawn
- 1999-04-06 JP JP2000609792A patent/JP2002541456A/en not_active Withdrawn
- 1999-04-06 WO PCT/US1999/007573 patent/WO2000060353A1/en not_active Application Discontinuation
- 1999-04-06 CA CA002368007A patent/CA2368007A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| EP1166111A1 (en) | 2002-01-02 |
| WO2000060353A1 (en) | 2000-10-12 |
| JP2002541456A (en) | 2002-12-03 |
| AU3475299A (en) | 2000-10-23 |
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