A device which can be used for filtering samples is described. The device is comprised of a plurality of filter wells, each having a wide region and a narrow region. The device is fitted with a filter element and then filled with a gel filtration matrix which is selected so that molecules of a particular molecular size will diffuse into the matrix. The device is centrifuged to remove water from the interstitial regions of the gel filtration matrix, and a sample is then added to the device containing the dried gel filtration matrix. The device is again centrifuged, causing smaller molecules to diffuse into the matrix and allowing larger molecules to exit the device, wherein they are collected and analyzed. The device is capable of filtering sample sizes as low as 1 L and can be used in a variety of existing laboratory equipment, including bench-top centrifuges and microcentrifuges. A process for using the device is also disclosed.
Use Of Additives For The Reduction Of Non-Specific Binding In Assays
A method for reducing non-specific binding in an assay is provided herein. The method includes (a) providing a reaction mixture, which includes or is suspected to include a first component and a second component capable of binding to each other in a specific binding reaction, and (b) adding non-physiological amounts of at least one additive to the reaction mixture before, during or after binding in a sufficient amount to reduce non-specific binding in the reaction mixture. The method further includes (c) monitoring or measuring the presence and/or concentration of at least one of the first and second components after step (b).
Use Of Additives To Lower The Rate Of A Binding Reaction
A method of lowering the rate of a specific binding reaction in an assay for the detection and/or measurement of an analyte of interest is provided herein. In particular, the method includes providing a fluorescent conjugate of the analyte; a component capable of specifically binding to the analyte and its fluorescent conjugate; and a sample, which includes or is suspected to include the analyte. The method also includes allowing the specific binding component to interact simultaneously or at different times with the fluorescent conjugate of the analyte and the analyte in the sample, thereby forming a detectable complex due to the reaction between the fluorescent conjugate of the analyte and its specific binding component, wherein the reaction is performed in the presence of non-physiological amounts of at least one additive. The method further includes monitoring for the rate of change of the concentration of the detectable complex as a function of the amount of analyte in the sample.
Device And Method Of Detecting Streptococcal Mutans
A device, kit and method for detecting oral bacteria are provided. The device is a tube, which includes on its inside surface a coating of an agar medium selective for growing gram-positive bacteria. The device is particularly suitable for detecting the extent of growth of which provides an indication of the susceptibility of a patient to dental caries.
Alpha-Amylase Assay And Substrates For Use Therein
Paul T. Nix - Jackson NJ Rebecca D. Goldfarb - Baltimore MD Linda J. Stong - Hightstown NJ Lorraine E. Sulick - Scotch Plains NJ Ramesh C. Trivedi - Freehold NJ Stanley W. Morgenstern - Neptune NJ
Assignee:
Worthington Biochemical Corporation - Freehold NJ
International Classification:
C12Q 154 C12Q 158 C12Q 140 C12P 1918
US Classification:
435 14
Abstract:
A maltodextrin phosphorylase limit dextrin in the presence of maltodextrin phosphorylase and inorganic phosphate, is used as a substrate for alpha-amylase, which initiates a series of enzymatic reactions resulting in a chromogen response which can be used to measure the concentration of alpha-amylase in a body fluid. A novel limit dextrin and its preparation also are described.
Method Of Determining Cystic Fibrosis Ciliostatic Factor
Thomas J. Kelleher - Springlake Heights NJ Paul T. Nix - Jackson NJ
Assignee:
CooperBiomedical, Inc. - Malvern PA
International Classification:
G01N 100 G01N 140
US Classification:
435 4
Abstract:
A method for detecting the presence of cystic fibrosis ciliostatic factor in mammalian body fluid comprises contacting an enzyme whose activity is inhibited by the factor with a substrate for the enzyme in the presence of the body fluid, the substrate being substantially resistant to reactions catalyzed by enzymes in the body fluid, whereby the substrate is converted by the enzyme at a measurable rate, and comparing the rate of substrate conversion with the rate of substrate conversion by the enzyme in the absence of cystic fibrosis ciliostatic factor.
4-Aminoantipyrine Dye For The Analytic Determination Of Hydrogen Peroxide
Paul T. Nix - Jackson NJ Spencer M. Fields - Red Bank NJ
Assignee:
Millipore Corporation - Bedford MA
International Classification:
C07D23148 C07D23146
US Classification:
548366
Abstract:
A 3-aminobenzoic acid or a 3-aminobenzenesulfonic acid, when reacted with a 4-aminoantipyrine in aqueous medium in the presence of hydrogen peroxide forms a novel colored dye which is believed to be a charge-transfer complex of free radicals formed from the 3-aminoaromatic acid and the 4-aminoantipyrine. The dye and the process by which it is produced are useful in analytical procedures for hydrogen peroxide, as well as in enzymatic analyses involving the formation of hydrogen peroxide.
Reagent And Method For The Analytic Determination Of Hydrogen Peroxide
Paul T. Nix - Jackson NJ Spencer Fields - Red Bank NJ
Assignee:
Millipore Corporation - Bedford MA
International Classification:
C12Q 162 C12Q 128
US Classification:
435 10
Abstract:
A 3-aminobenzoic acid or a 3-aminobenzenesulfonic acid, when reacted with a 4-aminoantipyrine in aqueous medium in the presence of hydrogen peroxide forms a novel colored dye which is believed to be a charge-transfer complex of free radicals formed from the 3-aminoaromatic acid and the 4-aminoantipyrine. The dye and the process by which it is produced are useful in analytical procedures for hydrogen peroxide, as well as in enzymatic analyses involving the formation of hydrogen peroxide.
Lakin Ragains, Matthew Loewenstein, Christa Gordon, Kryslyn Packard, Sheena Gordon, Jacob Gordon, Cory Stacey, Andres Contreras, Melissa Savely, Jill Schubert