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Determination of alpha-N-acetamino galactosidase activity

A technology of acetylaminosemi-glycosidase, applied in the direction of organic active ingredients, hydrolase, specific peptides, etc., can solve the problem of decreased activity of plasma Gc protein precursor

Inactive Publication Date: 2004-07-07
山本信人
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  • Abstract
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  • Application Information

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Problems solved by technology

Therefore, an increase in the activity of the patient's serum or plasma α-N-acetylgalactosaminidase will lead to a decrease in the activity of the precursor of the plasma Gc protein

Method used

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  • Determination of alpha-N-acetamino galactosidase activity
  • Determination of alpha-N-acetamino galactosidase activity
  • Determination of alpha-N-acetamino galactosidase activity

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Embodiment Construction

[0040] Description of method for cloning of gene encoding macrophage activating factor

[0041] A. Cloning the cDNA of the Gc protein into an insect virus

[0042] The full-length cDNA of bm human Gc protein was isolated from the human liver cDNA library of bacteriophage lambda gtll (Clontech, Palo Alto, CA) using the pico BlueTm immunoscreening kit from Stratagene of La Jolla, CA. There are several facts that illustrate the advantages of the polyhedrin expression system of the baculovirus in insect cells: (a) in the later stages of the infection cycle, the system contains more than half of the total cellular protein and is expressed at very high levels in infected cells (b) is not necessary for viral infection or replication, meaning that the recombinant virus does not require any auxiliary functions; (c) the virus lacking the polyhedron gene has a special plaque morphology derived from the virus containing the cloned gene; (d) Unlike bacterial cells, insect cells efficientl...

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Abstract

The vitamin D binding protein (Gc protein) and its small region (approximately 1 / 5 of the Gc peptide, known as region III) were cloned with the aid of baculovirus vectors. The cloned Gc protein and cloned domain (Cd) peptide were treated with immobilized β-galactosidase and sialidase to produce macrophage activating factors GcMAFc and CdMAF, respectively. These cloned macrophage activating factors and GcMAFs can be used to treat cancer, HIV infection, and osteoporosis, as well as as adjuvants for immunization and vaccination. Methods and antibody-sandwich ELISA kits for detecting serum or plasma α-N-acetylgalactosaminidase activity in patients with cancer and HIV infection were developed.

Description

[0001] This application is a divisional application of an invention patent application with an application date of June 5, 1996, an application number of 96195808.1, and an invention title of "macrophage activating factor derived from cloned vitamin D binding protein". technical field [0002] The present invention relates to the use of cloned vitamin D binding protein (Gc protein) and oligosaccharide digestion of cloned Gc protein domain III to produce potent macrophage activating factors and the role of these macrophage activating factors in various cancers, HIV applications in infection and osteoporosis, and as an adjuvant in immunizations and vaccinations, has also developed the use of a specific enzyme detected in the blood of cancer and HIV-infected patients, α-N-acetylaminosemi Diagnostic and prognostic methods of lactosinase. [0003] the term [0004] Gc protein vitamin D 3 binding protein [0005] MAF macrophage activating factor [0006] GcMAF Gc protein-derived...

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Application Information

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IPC IPC(8): A61K31/00A61K38/00A61K39/00A61P19/00A61P19/08A61P19/10A61P31/00A61P31/12A61P35/00C07K14/47C07K14/52C07K14/57C07K14/705C12N9/38C12N15/09C12N15/12C12N15/19C12P21/02C12Q1/34C12Q1/40G01N33/569G01N33/573G01N33/574
CPCG01N2333/16C12N9/2402C07K2319/00C07K14/57C07K14/47G01N33/57484G01N33/574G01N33/56983C12Y302/01049G01N33/56988G01N33/573C12Q1/34Y10S436/813C12N2799/026A61K38/00A61K39/00A61P19/00A61P19/08A61P19/10A61P31/00A61P31/12A61P35/00
Inventor 山本信人
Owner 山本信人
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