Test device for assays for hydrolytic enzyme activity

Chemistry: molecular biology and microbiology – Apparatus – Including measuring or testing

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435 18, 435 23, 435 34, 422 57, C12M 140, G01N 3122

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active

055852734

ABSTRACT:
A dry, self-contained test device for assaying for the presence of an enzymatically active hydrolase in a sample is disclosed. The test device combines a reporter enzyme immobilized on a solid support, an indicator, and all other reagents and components necessary to achieve a detectable indication of the presence or absence of the enzymatically active hydrolase in the sample. Preferred devices contain positive and negative controls as well.

REFERENCES:
patent: 4318986 (1982-03-01), Richardson et al.
patent: 5120718 (1992-06-01), Goldman
patent: 5132085 (1992-07-01), Pelanek
patent: 5156954 (1992-10-01), Mielke
patent: 5202233 (1993-04-01), Herrmann
patent: 5268146 (1993-12-01), Lawrence et al.
patent: 5288612 (1994-02-01), Griffin
Zherdev A. V., Method of Proteolytic Activity . . . ZH Microbiol Epidemiol Immunobiol vol. 1 Jan. 1988 pp. 51-55.
Kwon-Chung, K. J., et al., Genetic Evidence for Role of Extracellular Proteinase in Virulence of Candida albicans (Sep. 1985), Infection and Immunity, 571-575.
Crandall M., et al., Segregation of Proteinase-negative Mutants from Heterozygous Candida albicans (1987) (133), J. Gen. Microb, 2817-2824.
Cassone, A., et al., Evidence for a Correlation Between Proteinase Secretion and Vulvovaginal candiosis (Nov. 1987) 156(5), J. Infectious Diseases, 777-783.
Lott, T. J., et al., Nucleotide Sequence of the Candida albicans Aspartyl proteinase Gene (1989) 17(4), Nucleic Acids Res., 1779.
Edison, A. M., et al., Comparison of the Extracellular Proteinase Activity Produced by a Low-Virulence Mutant of Candida albicans and its Wild-Type Parent (May 1988), Infection and Immunity, 1388-1390.
Dunn, B. M., et al., The Synthesis, Purification and Evaluation of a Chromophoric Substrate for Pepsin and Other Aspartyl proteases: Design of a Substrate Based on Subsite Preferences (1984) 138, Analyt. Biochem., 68-73.
Dunn, B. M., et al., A Systematic Series of Synthetic Chromophic Substrates for Aspartic proteinases (1986) 237, 899-906.
De Bernardis, F., et al. Evidence for a Role for Secreted Aspartate Proteinase of Candida albicans in Vulvovaginal candidiasis (1990) 161, J. of Infectious Diseases, 1276-1283.
Raffi, R. O., et al., Proteins of Human Vaginal Fluid (Dec. 1977) 28(12), Fertility and Sterility, 1345-1348.
Pohl, J., et al., Chromophoric Peptide Substrates for Activity Determination of Animal Aspartic proteinases in the Presence of Their Zymogens: A Novel Assay (1983) 133, Anal. Biochem., 104-109.
Dunn, B. M., et al., The pH Dependence of the Hydrolysis of Chromogenic Substrates of the Type, Lys-Pro-Xaa-Yaa-Phe-(NO.sub.2)Phe-Arg-Leu, by Selected Aspartic proteinases: Evidence for Specific Interactions in Subsites S.sub.3 and S.sub.2 (1987) 913, Biochimica et Biophysica Acta, 122-130.
MacDonald, F., et al., Inducible Proteinase of Candida albicans in Diagnostic Serology and in the Pathogensis of Systemic Candidosis (1980) 13, J. Med. Microbiol., 423-435.
MacDonald, F., et al., Virulence for Mice of a Proteinase-secreting Strain of Candida albicans and a Proteinase-deficient Mutant (1983) 129, J. Gen. Microbiol., 431-438.
Ruchel, R., Properties of a Purified Proteinase from the Yeast Candida albicans (1981) 659, Biochimica et Biophysica Acta, 99-113.
Portillo, F., et al., Purification and Properties of Three Intracellular Proteinases from Candida albicans (1986) 881, Biochimica et Biophysica Acta, 229-235.
De Bernardis, F., et al., Isolation, Acid Proteinase Secretion, and Experimental Pathogenicity of Candida parapsilosis from Outpatients with Vaginitis (Nov. 1989) 27(11), J. Clin. Microbiol., 2598-2603.
Ray, T. L., et al., Comparative Production and Rapid Purification of Candida Acid Proteinase from Protein-Supplemented Cultures (Feb. 1990) 58(2), Infection and Immunity, 508-514.
De Bernardis, et al., Secretory Aspartate Proteinase in the Pathogenesis of Vaginitis Caused by Candida albicans (Anaheim, CA, 1990), Abstract No. F-91, Abstracts of the Annual Meetings of the American Society for Microbiology.
Crandall, M., et al., An EIA for Candida albicans Proteinase (1988), Abstract No. F-42, Abstracts of the Annual Meeting of the American Cancer Society for Microbiology.
Crandall, M., et al., Candida albicans Secreting Extracellular Proteinase Shows Increased Adherence to Endothelial Cell Monolayers (1984), Abstract No. F-24, Abstracts of the Annual Meeting of the American Cancer Society for Microbiology.
Zherdev A. V., et al., Method of Proteolytic Activity Determination Using Bovine Serum Albumin Conjugate (Jan. 1988) 1, ZH Microbiol. Epimeriol. Immunobiol., 51-55.
Toth, M. V., et al., A Simple, Continuous Fluoremetric Assay for HIV Protease (1990) 36, Int. J. Peptide Protein, 544-550.
Reesey, J., Biochemicals for Protein Research (1987) Biochemica Information. First Edition, 87-107.
Alderete, J. F., The Vagina of Women Infected with Trichomonas vaginalis Has Numerous Porteinases and Antibody to Trichomonad proteinases (Dec. 1991) 67(6), Genitourin Med., 469-474.
Capobianco, J., et al., Application of a Fluorogenic Substrate in the Assay of Proteolytic Activity and in the Discovery of a Potent Inhibitor of Candida albicans Aspartic Proteinase (1992) (204), Analytical Biochemistry, 96-102.

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