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United States Patent (19) 11) Patent Number: 4,520,110 Stryer Et Al

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United States Patent (19) 11) Patent Number: 4,520,110 Stryer Et Al United States Patent (19) 11) Patent Number: 4,520,110 Stryer et al. 45) Date of Patent: May 28, 1985 54) FLUORESCENT IMMUNOASSAY EMPLOYNG A PHYCOBILIPROTEIN OTHER PUBLICATIONS LABELED LIGAND OR RECEPTOR Hales et al., "Labeled Antibodies and Their Use in the Immunoradiometric Assay', Immunochemical Tech (75) Inventors: Lubert Stryer, Stanford; Alexander niques, vol. 7, Methods in Enzymology, 1980, pp. N. Glazer, Orinda; Vernon T. Oi, 334-355. Palo Alto, all of Calif. Kronick et al., “Immunoassay Techniques with Fluo (73) Assignee: The Board of Trustees of the Leland rescent Phycobiliprotein Conjugates', Clinical Chem., Stanford Junior University, Stanford, vol. 29, #9, 1983, pp. 1582-1586. Calif. OhEocha, Biochemistry, vol. 2, 1963, pp. 375-382. Stedman's Medical Dictionary, Williams & Wilkins, 21 Appl. No.: 454,768 Balt. 22nd Ed., 1972, pp. 154, 155, 318, 766, 1004 22 Filed: Dec. 30, 1982 Primary Examiner-Sidney Marantz Assistant Examiner-K. S. Moss Related U.S. Application Data Attorney, Agent, or Firm-Bertram I. Rowland 63 Continuation-in-part of Ser. No. 309,169, Oct. 6, 1981, 57 ABSTRACT abandoned. Sensitive detection techniques and compositions for 51) Int, Cl. ...................... G01N 33/54; G01N 31/00 such techniques employing fluorescent proteins having 52) U.S. Cl. .................................... 436/501; 436/546; bilin prosthetic groups as labels i.e. phycobiliprotein. 436/536; 436/519; 436/800; 424/7.1; 260/112 The bilin containing proteins can be conjugated to li R; 260/112 B gands or receptors for use in systems involving ligand 58) Field of Search ........................... 424/3, 7, 85, 89; receptor binding for the analysis, detection or separa 436/528,546.7, 805, 826, 500, 501, 519, 536, tion of ligands and receptors. Particularly, one or more 546,800; 260/112 R, 112 B of the bilin containing proteins may be used as labels in conjuction with each other or other fluorescers for 56) References Cited defining subsets of naturally occurring aggregations e.g. U.S. PATENT DOCUMENTS cells. 4,193,983 3/1980 Ullman ................................ 436/826 4,302,536 11/1981 Longenecker ...................... 436/826 4 Claims, 4 Drawing Figures U.S. Patent May 28, 1985 Sheet 1 of 4 4,520,110 HPLC OF PHYCOERYTHRIN-IgG (a) PE-S-S-IgG S (s CN s C 2 C 8 (b) PE-SH C (c) IgG-S-S-Pyr M O 4 8 2 is 20 24 F G .. MINUTES AFTER NJECTION U.S. Patent May 28, 1985 Sheet 2 of 4 4,520,110 STTIBOCIENIVf1S\7–9–Ed ÅLISNEJNIBONEOSEMJOOT [HTvOSOIwHLIHv?o-i] GI STTEOCJENIViSNn STTEO-JOHEEWTAN [LINnHad(ç_01)TwLoL30NOILovgº] U.S. Patent May 28, 1985 Sheet 3 of 4 4,520,110 PE-B-A STANED BEAD (YELLOW) FLUORESCEN AVDIN STANED BEAD (GREEN) FIG-3A U.S. Patent May 28, 1985 Sheet 4 of 4 4,520,110 PE-B-A STANED BEAD (ORANGE-RED) FIG.-3B 4,520,110 1 2 fluorescein. The impact of this deficiency is felt in the FLUORESCENT IMMUNOASSAY EMPLOYING A area of fluorescence-activated cell sorting. The full PHYCOBELPROTEIN LABELED LIGAND OR potential of this powerful and versatile tool has not yet RECEPTOR been realized because of limitations in currently avail 5 able fluorescent tags. Two and three-parameter fluores This invention was made with Government support cence sorting have not been effectively exploited, under NSF Grant No. PCM 79-10996 and NIH Grant largely because of the unavailability of good long wave Nos. GM-24032 and AI-06144. The Government has length emitting probes. certain rights in this invention. Other techniques, involving histology, cytology, im CROSS-REFERENCE TO RELATED 10 munoassays would also enjoy substantial benefits from APPLICATIONS the use of a fluorescer with a high quantum efficiency, This is a continuation-in-part patent application of absorption and emission characteristics at longer wave application Ser. No. 309,169, filed Oct. 6, 1981 now lengths, having simple means for conjugation and being abandoned. 15 substantially free of non-specific interference. BACKGROUND OF THE INVENTION SUMMARY OF THE INVENTION Field of the Invention Proteins with bilin prosthetic groups are employed as Fluorescent probes are valuable reagents for the anal fluorescent labels in systems involving ligand-receptor ysis and separation of molecules and cells. Some specific 20 reactions. The billiproteins are readily conjugated, pro examples of their application are: (1) identification and vide for high quantum efficiency with absorption and separation of subpopulations of cells in a mixture of cells emission at long wavelengths in the visible, and enhance by the techniques of fluorescence flow cytometry, the sensitivity and accuracy of methods involving li fluorescence-activated cell sorting, and fluorescence gand-receptor reactions. The billiproteins may be used microscopy; (2) determination of the concentration of a 25 individually, in combination, or together with non Substance that binds to a second species (e.g., antigen proteinaceous fluorescers. antibody reactions) in the technique of fluorescence BRIEF DESCRIPTION OF THE DRAWINGS immunoassay; (3) localization of substances in gels and other insoluble supports by the techniques of fluores FIG. 1 shows the high pressure liquid chromato cence staining. These techniques are described by Her 30 grams of phycoerythrin-immunoglobulin conjugate Zenberg et al., "Cellular Immunology," 3rd ed., chapt. (PE-S-S-IgG) and the reactant precursors thereof, thi 22, Blackwell Scientific Publications, 1978 (fluores olated phycoerythrin (PE-SH) and activated immuno cence-activated cell sorting); and by Goldman, “Fluo globulin (IgG-S-S-Pyr). rescence Antibody Methods,' Academic Press, New FIG. 2 shows the fluorescence-activated cell sorter York, 1968 (fluorescence microscopy and fluorescence 35 analysis of a cell population containing spleen cells staining). bearing PE-B-A stained anti-IgG immunoglobulin. When employing fluorescers for the above purposes, FIG. 3a shows the visualization of a mixture of aga there are many constraints on the choice of the fluo rose beads containing a labeled anti-immunoglobulin by rescer. One constraint is the absorption and emission fluorescence microscopy utilizing standard fluorescein characteristics of the fluorescer, since many ligands, emission filter combinations, wherein some beads were receptors, and materials associated with such con labeled with PE-B-A and some beads were labeled with pounds in the sample in which the compounds are found fluorescein-avidin. e.g. blood, urine, cerebrospinal fluid, will fluoresce and interfere with an accurate determination of the fluores FIG. 3b shows the visualization of the same cell pop cence of the fluorescent label. Another consideration is 45 ulation as in FIG. 3a under fluorescence microscopy the ability to conjugate the fluorescer to ligands and utilizing a red filter combination. receptors and the effect of such conjugation on the DESCRIPTION OF THE SPECIFIC fluorescer. In many situations, conjugation to another EMBODIMENTS molecule may result in a substantial change in the fluo Compositions are provided comprising billiproteins, Tescent characteristics of the fluorescer and in some 50 cases, substantially destroy or reduce the quantum effi (the term “biliproteins” is equivalent to the term ciency of the fluorescer. A third consideration is the "phycobiliproteins”) conjugated to a member of a spe quantum efficiency of the fluorescer. Also of concern is cific binding pair, said pair consisting of ligands and whether the fluorescent molecules will interact with receptors. These compositions find use for labeling by each other when in close proximity, resulting in self 55 non-covalent binding to the complementary member of quenching. An additional concern is whether there is the specific binding pair. A wide variety of methods non-specific binding of the fluorescer to other com involve competitive or non-competitive binding of li pounds or container walls, either by themselves or in gand to receptor for detection, analysis or measurement conjunction with the compound to which the fluorescer of the presence of ligand or receptor. Many of these is conjugated. 60 techniques depend upon the presence or absence of The applicability and value of the methods indicated fluorescence as a result of non-covalent binding of the above are closely tied to the availability of suitable labeled member of the specific binding pair with its fluorescent compounds. In particular, there is a need for complementary member. fluorescent substances that emit in the longer wave The conjugates of the subject invention are bili length visible region (yellow to red). Fluorescein, a 65 proteins bound either covalently or non-covalently, widely used fluorescent compound, is a useful emitter in normally covalently, to a particular ligand or receptor. the green. However, the conventional red fluorescent The billiproteins have a molecular weight of at least label rhodamine has proved to be less effective than about 30,000d., (d-daltons) more usually at least about 4,520,110 3 4. 40,000d, and may be as high as 600,000 or more daltons plement factors, lymphokines, mucoproteins, polysialic usually not exceeding about 300,000d. acids, chitin, collagen, keratin, etc. The billiproteins will normally be comprised of from 2 Depending upon the molecule being labeled, a wide to 3 different subunits, where the subunits may ranged variety of linking groups may be employed for conju from about 10,000 to about 60,000 molecular weight. gating the billiprotein to the other molecule. For the The billiproteins are normally employed as obtained in most part, with small molecules, those under 2,000 mo their natural form from a wide variety of algae and lecular weight, the functional group of interest for link cyanobacteria. The presence of the protein in the bili ing will be carbonyl, either an aldehyde to provide for proteins provides a wide range of functional groups for reductive amination or a carboxyl, which in conjunc conjugation to proteinaceous and non-proteinaceous 10 tion with carbodiimide or as an activated ester e.g. molecules. Functional groups which are present include N-hydroxy succinimide, will form a covalent bond with amino, thio and carboxy.
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