AU628295B2 - Fluorescent label - Google Patents
Fluorescent label Download PDFInfo
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- AU628295B2 AU628295B2 AU23422/88A AU2342288A AU628295B2 AU 628295 B2 AU628295 B2 AU 628295B2 AU 23422/88 A AU23422/88 A AU 23422/88A AU 2342288 A AU2342288 A AU 2342288A AU 628295 B2 AU628295 B2 AU 628295B2
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- Prior art keywords
- chlorophyll
- fluorescent probe
- protein
- proteins
- water
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- 239000007850 fluorescent dye Substances 0.000 title claims description 22
- 101001090094 Arabidopsis thaliana Kunitz trypsin inhibitor 2 Proteins 0.000 claims description 12
- 108090000623 proteins and genes Proteins 0.000 claims description 12
- 102000004169 proteins and genes Human genes 0.000 claims description 12
- 238000000034 method Methods 0.000 claims description 11
- 239000003446 ligand Substances 0.000 claims description 5
- 230000009870 specific binding Effects 0.000 claims description 5
- 229930002875 chlorophyll Natural products 0.000 claims description 4
- 235000019804 chlorophyll Nutrition 0.000 claims description 4
- ATNHDLDRLWWWCB-AENOIHSZSA-M chlorophyll a Chemical compound C1([C@@H](C(=O)OC)C(=O)C2=C3C)=C2N2C3=CC(C(CC)=C3C)=[N+]4C3=CC3=C(C=C)C(C)=C5N3[Mg-2]42[N+]2=C1[C@@H](CCC(=O)OC\C=C(/C)CCC[C@H](C)CCC[C@H](C)CCCC(C)C)[C@H](C)C2=C5 ATNHDLDRLWWWCB-AENOIHSZSA-M 0.000 claims description 4
- 238000003018 immunoassay Methods 0.000 claims description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 4
- 241000199914 Dinophyceae Species 0.000 claims description 3
- 230000027455 binding Effects 0.000 claims description 3
- 235000021466 carotenoid Nutrition 0.000 claims description 3
- 150000001747 carotenoids Chemical class 0.000 claims description 3
- 239000003153 chemical reaction reagent Substances 0.000 claims description 3
- 239000000470 constituent Substances 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 24
- 108010004729 Phycoerythrin Proteins 0.000 description 9
- 239000000523 sample Substances 0.000 description 8
- 241000196324 Embryophyta Species 0.000 description 5
- 239000000427 antigen Substances 0.000 description 4
- 108091007433 antigens Proteins 0.000 description 4
- 102000036639 antigens Human genes 0.000 description 4
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 4
- 238000010166 immunofluorescence Methods 0.000 description 4
- 108060006184 phycobiliprotein Proteins 0.000 description 4
- 241000195493 Cryptophyta Species 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 3
- 238000003306 harvesting Methods 0.000 description 3
- 230000003287 optical effect Effects 0.000 description 3
- 108020003175 receptors Proteins 0.000 description 3
- 230000000638 stimulation Effects 0.000 description 3
- JWDFQMWEFLOOED-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 3-(pyridin-2-yldisulfanyl)propanoate Chemical compound O=C1CCC(=O)N1OC(=O)CCSSC1=CC=CC=N1 JWDFQMWEFLOOED-UHFFFAOYSA-N 0.000 description 2
- 241000199919 Phaeophyceae Species 0.000 description 2
- 238000000862 absorption spectrum Methods 0.000 description 2
- 230000008033 biological extinction Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000003599 detergent Substances 0.000 description 2
- 210000004698 lymphocyte Anatomy 0.000 description 2
- 239000004005 microsphere Substances 0.000 description 2
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 2
- 238000006552 photochemical reaction Methods 0.000 description 2
- 241000200158 Amphidinium Species 0.000 description 1
- 241000200155 Amphidinium carterae Species 0.000 description 1
- 241000206761 Bacillariophyta Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108010041397 CD4 Antigens Proteins 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 241000206751 Chrysophyceae Species 0.000 description 1
- 241000924360 Glenodinium Species 0.000 description 1
- 241000200139 Gonyaulax Species 0.000 description 1
- 108010059332 Photosynthetic Reaction Center Complex Proteins Proteins 0.000 description 1
- 241001482237 Pica Species 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- UYRDHEJRPVSJFM-VSWVFQEASA-N [(1s,3r)-3-hydroxy-4-[(3e,5e,7e,9e,11z)-11-[4-[(e)-2-[(1r,3s,6s)-3-hydroxy-1,5,5-trimethyl-7-oxabicyclo[4.1.0]heptan-6-yl]ethenyl]-5-oxofuran-2-ylidene]-3,10-dimethylundeca-1,3,5,7,9-pentaenylidene]-3,5,5-trimethylcyclohexyl] acetate Chemical compound C[C@@]1(O)C[C@@H](OC(=O)C)CC(C)(C)C1=C=C\C(C)=C\C=C\C=C\C=C(/C)\C=C/1C=C(\C=C\[C@]23[C@@](O2)(C)C[C@@H](O)CC3(C)C)C(=O)O\1 UYRDHEJRPVSJFM-VSWVFQEASA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 125000000909 amidinium group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 229930002868 chlorophyll a Natural products 0.000 description 1
- 108091000085 chlorophyll binding Proteins 0.000 description 1
- 239000001752 chlorophylls and chlorophyllins Substances 0.000 description 1
- 210000003763 chloroplast Anatomy 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 238000005286 illumination Methods 0.000 description 1
- 238000003125 immunofluorescent labeling Methods 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 238000011527 multiparameter analysis Methods 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- UTIQDNPUHSAVDN-UHFFFAOYSA-N peridinin Natural products CC(=O)OC1CC(C)(C)C(=C=CC(=CC=CC=CC=C2/OC(=O)C(=C2)C=CC34OC3(C)CC(O)CC4(C)C)C)C(C)(O)C1 UTIQDNPUHSAVDN-UHFFFAOYSA-N 0.000 description 1
- 230000000243 photosynthetic effect Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000006479 redox reaction Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 210000002377 thylakoid Anatomy 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
- G01N33/531—Production of immunochemical test materials
- G01N33/532—Production of labelled immunochemicals
- G01N33/533—Production of labelled immunochemicals with fluorescent label
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/44—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from protozoa
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Urology & Nephrology (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Hematology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Cell Biology (AREA)
- Genetics & Genomics (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Investigating, Analyzing Materials By Fluorescence Or Luminescence (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Description
I
Form PATENTS ACT 1952 COMPLETE SPECIFICATION
(ORIGINAL)
FOR OFFICE USE Short Title: Int. CI: Application Number: Lodged: .Cipnplete Specification-Lodged: eeAccepted: Lapsed: :Published: Priority: 0 At 41 d Art: eof Applicant: Ad~dress of Applicant: Actual Inventor: TO BE COMPLETED BY APPLICANT DR. MARK WILSON Address for Service: -65-EI~tKSEN-AVENUE pf O A4ZTA-RM9N N SW 64 Complete Specification for the invention entitled: FLUORESCENT LABEL The following statement is a full description of this invention, including the best method of performing it known to me-* Note: The description is to be typed in double spacing, pica type %lace, in an area not exceeding 250 mm in depth and 160 mm i width, on tough white paper of good r-nlity and it Is to be inserted inside this ;orm.
14599/78- L Printed by C. J. Tio?~ipsoN, Commonwealth Government Printer, Cinberra li The present invention relates to fluorescent probes incorporating a novel fluorescent label.
Fluorescent probes are valuable reagents for the analysis and separation of molecules and cells. One type of probe, which has been extensively studied is fluorescently labelled antibodies. To date, these probes consist of an antibody conjugated with, for example, fluorescein or a phycobiliprotein, such as phycoerythrin. Under appropriate optical stimulation, 10 fluorescein emits green light whilst phycoerythrin emits orange light.
The technique of detecting the presence of antigens by immunofluorescence, and the use of fluorescently labelled antibodies is well known in the art. This 15 technique traditionally involves reacting a sample containing a particular antigen with a fluorescently 0 labelled antibody directed against the antigen, and then measuring the amount of bound fluorescence. As cells .possess characteristic antigenic determinants which enable cell types to be distinguished, immunofluorescence has been used to determine the presence or number of a particular type of cell in a given sample.
This principle of using immunofluorescence to determine the number of a particular cell sub-type in a population is applied in the method and apparatus disclosed in U.S. patent NO. 4284412. This patent is directed toward an automated method of identifying and enumerating cells of a selected sub-class and to an r apparatus for carrying out such a method. This method involves contacting a blood sample with a fluorescently labelled antibody directed against a selected sub-class of lymphocytes. The red cells are then lysed and the sample passed through a zone, substantially one cell at a time, where the cells are exposed to illumination of a wavelength at which the labelled antibody fluoresces.
The cells are then differentiated on the basis of their fluorescence.
10 At present, there exists the need for new fluorescent probes incorporating a fluorescent label which emits at a different wavelength to either fluorescein or .phycoerythrin. Apart from the obvious benefits to be gained by increased choice of labels, such a new label would be of particular value in situations where multiparameter analysis is required. The provision of a third fluorescent label would enable a sample to be contacted with three probes each directed against c distinct antigen and each labelled with a different fluorescent label. This would enable the detection of three distinct antigenic determinants on the one cell.
All photosynthetic organisms have some form of lightharvesting complex designed to trap light of particular wavelengths for use in photochemical reactions. In the general scheme of events, one component of the lightharvesting complex will absorb light at a particular wavelength and pass on the absorbed energy to the next member in the complex until finally the energy reaches the photochemical reaction centre, where it is used in 2i redox reactions leading to carbon fixation and the synthesis of sugars. In some cases, when components of a light-harvesting complex are removed from their in situ position they will still absorb light (with a characteristic absorption spectrum) but, now being uncoupled from the remainder of the photosynthetic complex, they emit the absorbed energy as light of a different, longer wavelength.
The nature of the light-harvesting complexes varies 4 10 from one group to the next. The red and blre-green algae use their phycobiliproteins for this purpose and phycoerythrin, a member of the complex in these groups, is now widely used as a fluorescent label. The carotenoid-chlorophyll-proteins are light-harvesting 15 complexes found in brown algae, diatoms, dinoflagellates and chrysophytes. Relative to the phycobiliproteins, Svery little work has been done studying these Sstructures. Like the phycobiliproteins, these complexes are found associated with the thylakoid membranes of the chloroplast. Within the groups of algae mentioned above, the complexes differ widely both in terms of their molecular weights and the chlorophylls and carotenoids with which they are associated. Some of the complexes are water soluble, while others can be made so by treatment with detergents.
In a first aspect the present invention consists in a fluorescent probe comprising a water-soluble chlorophyll-protein conjugated either covalently or noncovalently to a member of a specific binding pair where said pair consists of ligand and receptor.
In a second aspect the present invention consists in an improved fluorescent immunoassay employing as a reagent a fluorescent compound conjugated either covalently or non-covalently to a member of a specific binding pair where said pair consists of ligand and receptor, and said immunoassay is for the determination of a member, the binding of the conjugate to a member being indicative of the presence of said member, the 10 improvement comprising employing in said assay a fluorescent compound comprising a water-soluble chlorophyll-protein.
*.In a third aspect the present invention consists in an automated method of identifying and enumerating 15 cells of a select sub-class of lymphocytes in blood comprising the steps of:- .C providing an aliquot from the blood to be studied; 060 selectively tagging cells of said class by S3 20 incubating said aliquot with a fluorescently 0 labelled antibody which is selectively reactive with distinct antigenic determinants on the sairface of cells of said sub-class, said antiuody having a predetermined fluorescence response to a given optical stimulation; lysing red cells from said aliquot; passing said aliquot, substantially a cell at a time, through an area of focussed optical stimulation of said given type, while detecting 4 iY P~PYsPes~:-7~ i light scattered and emitted from said cells; and differentiating cells of said sub-class based at least in part on occurrence of said predetermined fluorescence response in said detected light, characterised in that the fluorescent label is a water-soluble chlorophyll-protein.
In a preferred embodiment of the present invention the water-soluble chlorophyll-proteins have a molecular 10 weight of at least ten kilodaltons.
The water-soluble chlorophyll-proteins which are used as the fluorescent label in the present invention are exemplified by the carotenoid chlorophyll-proteins.
These proteins can be excited in the range of 400 550 15 nm and emit at about 675 nm (a Stokes shift of 200 nm). This means that they could be excited by a laser at 488 nm and the emission measured independently of Sthose of fluorescein and phycoerythrin. In other words, ,they could function for users of a single laser flow cytometer as a third colour label. Furthermore, their high absorption coefficients would make them competitive with or superior to phycoerythrin for use in immunofluorescence studies of any kind. Particular examples of carotenoid-chlorophyll-proteins are fucoxanthin-chlorophyll a,c-protein from the diatom Phaedoactylum tricornutum (Friedman Alberte, 1984, Plant Physiol. 76:483-489), the violaxanthinchlorophyll-protein and the fucoxanthin-chlorophyllprotein from the brown seaweed Acrocarja .aniculata I(_~~iiclM~l;n___I i;.Ii
S.
S
SS
SS
0O
S.
0 0 S (Barrett Anderson, 1980, Biochimica et Biophysica Act 590:309-323), and the peridinin-chlorophyll-protein from the dinoflagellates Amphidinium, Gonyaulax and Glenodinium (Haxo et al, 1976, Plant Physiol. 57:297- 303, and Prezelin Haxo, 1976, Plant 128:133-141).
The carotenoid-chlorophyll proteins would be of particular value to all users of flow cytometers, particularly in situations where multiparameter anlaysis is desired.
10 There are a number of other chlorophyll-proteins in higher plants, algae and bacteria. Where these proteins are insoluble in water it is possible they may be made so by treatment with detergents. It is intended that such water-soluble chlorophyll-proteins are included within the scope of the present invention.
According to the present invention, the water-soluble chlorophyll-protein is bound either covalently or noncovalently, normally covalently, to a particular ligand or receptor of the specific binding pair.
In a particularly preferred embodiment of the present invention the water-soluble chlorophyll-protein is the peridinin-chlorophyll a-protein from the marine dinoflagellate Amidinium carterae. Purification ind partial characterisation of this protein has been described previously in the literature referred to above. This chromoprotein has a molecular weight of about 39 kd. and consists of a protein non-covalently associated with peridinin and chlorophyll a. The absorption spectrum for peridinin-chlorophyll a-protein
_J
.I is shown in Figure 1. Its fluorescence emission is maximum at about 675 nm. The molecular weight and extinction coefficient of peridinin-chlorophyll aprotein (PCP) is shown compared with the corresponding values for phycoerythrin (PE) and fluorescein isothiocyanate (FITC) in Table 1.
TABLE 1 S. S S S *5 S.
S
0
S
5 *5
S
S
S.
5 10 FLUORESCENT MOL. WT. EXTINCTION COEFFICIENT
LABEL
PCP 40,000 8.7 X 100 M- 1 cm- 1 (76 nm) PE 240,000 2.4 x 106 M- cm- 1 (565 nm) FITC 389.4 7.2 x 104 M- 1 cm-' (485 nm) In order that the nature of the present invention may be more clearly understood a preferred form thereof will now be described with reference to the following example.
20 EXAMPLE Isolation of peridinin-chlorophyll a protein (PCP) Amphidinium carterae is grown in culture vessels and the cells harvested by centrifugation and disrupted by two passes through a French press. The cell homogenate is then freed of cell debris by centrifugation and the PCP purified by a combination of gel filtration and ionexchange chromatography (Haxo et al, 1976, Plant Physiol. 57,:297-303) or Hydroxyapatite Chromatography together with ion-exchange
I
I MWchromatography.
Small amounts of partially purified PCP have been covalently bound to polyacrylamide microspheres. These microspheres fluoresce when viewed in a fluorescence microscope or run through a flow cytometer (Figure 2).
It is intended to conjugate PCP with an antibody, and demonstrate specific immunofluorescence staining. It is intended that by using N-succinimidyl 3-(2pyridyldithio) propionate (SPDP), PCP will be covalently 10 attached to a monoclonal antibody (e.g.AMD-RPA-T4, a monoclonal antibody which reacts with the CD4 antigen on S* the surface of peripheral blood lymphocytes). When the T4-PCP conjugate is reacted with peripheral blood lymphocytes and the cells run through a flow cytometer, 15 the CD4-positive cells are detected by red fluorescence of the T4-PCP conjugate specifically associated with their surfaces. The same cells reacted with an a*f irrelevant antibody conjugated with PCP will not show any specific red fluorescence.
As would be readily envisaged by the person skilled in the art similar methods could be used with virtually any antibody (monoclonal or polyclonal) or ligand (e.g.
streptavidin).
Claims (9)
1. Water soluble carotenoid chlorophyll proteins having a molecular weight of at least ten kilodaltons and which can be excited by light in the range of 400 to 500 nm and which emit light at about 675 nm when used as a constituent of a fluorescent probe.
2. A fluorescent probe comprising water soluble corotenoid chlorophyll proteins that include the peridin chlorophyll protein from the marine dinoflagellate Amphidinum carterae.
3. A fluorescent probe comprising the proteins of either claim 1 or 2 wherein the water-soluble chlorophyll protein is conjugated covalently or non-covalently with an antibody which has binding specificity to a third protein.
4. A fluorescent probe comprising the proteins of either claim 1 or 2 wherein the water-soluble chlorophyll protein is conjugated covalently with an antibody specific to said water-soluble chlorophyll protein.
5. A fluorescent probe according to claim 3 wherein the antibody is a member of a specific binding pair wherein said pair consists of ligand and receptor.
6. A fluorescent immunoassay employing as a reagent a fluorescent probe comprising a water soluble chlorophyll protein according to claim 5 and wherein said immunoassay is for the determination of a member, the binding of the conjugate to said R member being indicative of the presence of said member. _I I
7. An automated method of identifying and enumerating cells of a select sub-class wherein said cells are tagged with a specific binding paid as defined in claim
8. A fluorescent probe substantially as herein described with reference to the examples.
9. An automated method of identifying and enumerating cells of a select sub-class substantially as herein described with reference to the examples. D C *o L
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU23422/88A AU628295B2 (en) | 1987-10-06 | 1988-10-04 | Fluorescent label |
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AUPI474487 | 1987-10-06 | ||
| AUPI4744 | 1987-10-06 | ||
| AU23422/88A AU628295B2 (en) | 1987-10-06 | 1988-10-04 | Fluorescent label |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU2342288A AU2342288A (en) | 1989-04-06 |
| AU628295B2 true AU628295B2 (en) | 1992-09-17 |
Family
ID=25618960
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU23422/88A Ceased AU628295B2 (en) | 1987-10-06 | 1988-10-04 | Fluorescent label |
Country Status (1)
| Country | Link |
|---|---|
| AU (1) | AU628295B2 (en) |
-
1988
- 1988-10-04 AU AU23422/88A patent/AU628295B2/en not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| AU2342288A (en) | 1989-04-06 |
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