Process for the quantitative determination of the function and a

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

435 792, 435 13, 435214, 435215, 435217, 436501, 436512, 436518, 436819, G01N 3353, G01N 33566, C12Q 156, C12N 974

Patent

active

052984010

DESCRIPTION:

BRIEF SUMMARY
BACKGROUND OF THE INVENTION

The concentration of biologically significant substances in various liquids, such as blood, urine, fluids or others, is usually determined through two totally different methods. On the one hand through various determined (antigenic concentration). Such methods include made known (antigenic concentration); such methods include the radioimmunoassay (Travis, J. C., Clinical Radioimmunoassay, State of the Art, Radioassay, Ligand assay Publishers, Anaheim, Calif. 1980), the enzyme-linked-immunosorbent-assay (Nakamura, R. M., Dito, W. R. Tucker II E. S., Immunoassays in the Clinical Laboratory, Laboratory and Research Methods in Biology and Medicine, Vol. 3, Alan A. Liss Inc., New York, 1979; Voller, A., Bidwell, D. E., Bartlett, A., The Enzyme Linked Immunosorbent Assay - ELISA, The Authors, 1979, London; Langone,J. J., Van Vunakis, H., Methods in Enzymology, Immunochemical Techniques Part E, 1983, Academic Press; further Schuurs et al., U.S. Pat. No. 29,169 and Schuurs et al. , U.S. Pat. No. 4 016 043 )or coarse methods (Nakamura, R. M., Dito, W. R. Tucker III, E. S. Immunoassays in the Clinical Laboratory, Laboratory and Research Methods in Biology and Medicine, Vol. 3, Alan R. Liss Inc., New York, 1979; Langone, J. J., Van Vunakis, H., Methods in Enzymology, Immunochemical Techniques Part B, 1981, Academic Press), such as immunonephelometry, radial immunodiffusion or other appropriate immuno-precipitation processes. With the aid of immunological determination, it is possible to establish the concentration of a substance. However, it is impossible to draw any conclusion as to the function of this so-established substance. It has been proven frequently that, in various cases, in a normally immunologically determinable concentration, the function of this molecule did not correspond to the one immunologically determined and often was well below the normal value. As is the case with such molecules in proteins, having a precise enzymatic function or a carrier or cofactor function or the like in the body fluid and whose function is impaired by modifications in certain molecular fragments or which are inhibited by fixation to inhibitors.
The second possibility to establish the concentration of a certain substance in body fluids is the determination of the function of this substance (Bernmeyer, H. U., Methods of Enzymatic Analysis, Vol. 5 Verlan Chemie, 1984). Thereby, various systems are used, most of them being based on an enzyme reaction and which measure the enzymatic activity of the desired substance (Lorand, L., Proteolytic Enzymes, Methods in Enzymology, Vol. 45, 1976, Academic Press). By selecting specifically suitable substrates (e.g. high-molecular natural substrates, which are transformed by enzymes, such as fibrinogen for its enzyme thrombin, fibrin as substrate for plasmin, plasminogen as substrate for plasminogen activators, kininogen as substrate for kallikrein , but also low-molecular substrates, which contain the specific peptide compound for the respective enzyme and whose decomposition can lead, for instance, to a color reaction) and suitable determination criteria (thereby in the case of active enzyme formation, in the first stage the respectively formed enzymes are measured, respectively in the case of low-molecular substrates, the colored products, resp. newly formed or lost characteristics of substrates, such as the capability to form a bond with certain substances. An example of the los of such capability is the binding of the active plasminogen activator-inhibitor to its binding protein, whereby this binding capability is lost in the deactivation of the plasminogen activator-inhibitor. Further examples for these assaying processes involve binding to specific inhibitors, transfer proteins or other binding proteins, which can be correspondingly marked and be traced through a coupled reaction. It is possible to obtain a relatively high specificity for the determined substance; however, it is impossible to indicate a measured value with absolute specificity, since nor

REFERENCES:
patent: Re29169 (1980-01-01), Schuurs et al.
patent: Re31006 (1982-08-01), Schuurs et al.
patent: 4016043 (1977-04-01), Schuurs et al.
patent: 4563420 (1986-01-01), Verheijen
patent: 4629694 (1986-12-01), Harpel
patent: 4690890 (1987-09-01), Loor et al.
patent: 4707443 (1987-11-01), Nelson et al.
patent: 4849353 (1989-07-01), Harpel
Chap. 12, Immunochemistry (Ed Weir et al. pp. 12.8 & 12.9 (1986).
Parham, P., "Preparation and Purification of Active Fragments . . . ", Immunochemistry(Ed Weir et al.), pp. 14.1, 14.2 & 14.7 (1986).
Kroninger et al, Chem Absts. 104:182106k (1986).
Friguet et al., "A Convenient Enzyme Linked Immunosorbent Assay for Testing Whether Monoclonal Antibodies Recognize the Same Antigonic Site," Inj Immunoenzymatic Techniques, ed. S. Auramuas et al., Elsevior Science Publishers B.V., Amsterdam, Neth., 171-174 (1983).
C. Kluft, Tissue Plasminogen Activator, CRC (1988) Boca Raton, Florida, p. 102.
C. W. Francis et al, Physiologic Regulation and Pathologic Disorder of Fibrinolysis, J. B. Lippincott Co. Philadelphia, 1987.
Plasminogen Activators, North-Holland Publishing Co. Amsterdam, N.Y. Oxford 1977.
The Plasminogen-Plasmin Enzyme System, p. 349, Robbins, J.B. Lippincott Co. Philadelphia, 1987.
Chem. Abstracts 104:182106k (1986).
Bergemyer, Methods of Enzymatic Analysis, vol. V, pp. 425-433.
Bidwell, V. A. et al, The Enzyme Linked Immunosorbent Assay (Elisa) p. 3 (1977).
Travis, Jeffrey C., Clinical Radioimmunoassay . . . State of the Art 1st Edition (1980).
Nakamura, R. M. et al, Immunoassays in the Clinical Laboratory (1978).
Langone, John J., Methods in Enzymology, vol. 73, Immunochemical Techniques, Part B (1981).
Langone, John J., Methods in Enzymology, vol. 92, Immunochemical Techniques, Part E (1983).
Lorand, Laszlo, Methods in Enzymology, vol. XLV, Proteolytic Enzymes, Part B (1976).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Process for the quantitative determination of the function and a does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Process for the quantitative determination of the function and a, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Process for the quantitative determination of the function and a will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-790881

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.