32 results about "Bovine spongiform encephalopathy" patented technology

The invention provides cloned transgenic ungulates (e.g., bovines) in which prion protein activity is reduced by one or more genetically engineered mutations. Desirably, these transgenic bovines are also genetically modified to express xenogenous (e.g., human) antibodies. Because of their resistance to prion-related diseases such as bovine spongiform encephalopy (also known as mad cow disease), these bovines are a safer source of human antibodies for pharmaceutical uses and a safer source of agricultural products.

The invention discloses a method for preparing sheep enoxaparin sodium from sheep intestinal mucosa heparin. The method comprises the following steps: 1, preprocessing sheep heparins; 2, preparing a sheep heparin quaternary ammonium salt; 3, preparing sheep heparin benzyl ester; and 4, carrying out alkali depolymerization on the sheep heparin benzyl ester, decoloring, neutralizing by using an acid, carrying out alcohol precipitation, refining, and drying to obtain finished sheep enoxaparin sodium. The simple and efficient method for preparing the sheep enoxaparin sodium from the sheep intestinal mucosa heparin is screened and established, and researches of the systemic physical and chemical properties, the biological activity and the molecule structure are carried out on the prepared sheep enoxaparin sodium. The sheep enoxaparin sodium prepared in the invention completely accords with USP37 and EP8.0 quality release criteria of sheep enoxaparin sodium, and has extremely high practical values and medical application prospect. The sheep enoxaparin sodium has the advantages of simple and easily available raw material, controllable quality, no existence of bovine spongiform encephalopathy virus risk, promotion of the effective utilization of sheep culture and slaughter wastes (intestinal mucosa), and great economy potential.

A family of PCR assays is disclosed for determining, both qualitatively and quantitatively, presence of material from a predetermined species source and for quantifying the amount of such material. The assays are based respectively on SINEs uniquely characteristic of pig species, cow species, chicken species, and ruminant sub-order, and having a high copy number. The assays disclosed permit rapid, inexpensive evaluation of meat samples to facilitate elimination from their diet of pork or beef by persons desiring to avoid such food sources; as well as the assay of cattle feed to determine presence therein of ruminant-source proteins, which are a potential source of bovine spongiform encephalopathy (BSE), commonly referred to as “mad cow disease.” The assays amplify the predetermined unique SINEs and the resulting amplified mixture is then evaluated qualitatively by electrophoresis on gel containing ethidium bromide or quantitatively by SYBR Green-based detection or TaqMan chemistry. The invention also extends to kits, primers, and other products used in connection with the assays. The amplicons are selected to be from about 100 to 170 bp long.

The present invention is directed to the assessment of transmissible spongiform encephalopathy (TSE) using a sample from a living individual. The assessment is based on the use of an RNA marker molecule in a sample of whole blood. The RNA encodes a hypothetical cystein protease. The invention is further directed to the detection of the marker molecule by means of real-time PCR. The invention provides the use of the nucleotide sequence as a marker in the assessment of TSE, a method for assessing bovine spongiform encephalopathy (BSE) in a bovine animal as well as kits to practice the invention.

The present invention provides a method of detecting abnormal serum nucleic acid profiles to assess the risk of a transmissible spongiform encephalopathy, e.g., BSE.

A highly sensitive method for detecting prions in a sample is provided. These methods can be used to diagnose prion-mediated transmissible spongiform encephalopathy, such as bovine spongiform encephalopathy, Creutzfeldt-Jakob disease, scrapie or chronic wasting disease. In particular, methods for continuous automated cyclic expansion of prions are disclosed. The method is fast and highly sensitive, making it ideal for high-throughput testing.

Proteins expressed from within the prion protein genes of all animals and humans, "prionins", against which reagents can be prepared for accurate pre-symptomatic diagnosis, for detecting latent TSE, for detecting TSE contamination of food, blood and blood products and for therapeutic treatment of Bovine spongiform encephalopathy (BSE) in cows, Scrapie disease in sheep and Creutzfeldt-Jakob syndrome in humans, are revealed.

A specific, non-synonymous SNP in the Prnp gene encoding the bovine prion protein affects the susceptibility of bovine animals to bovine spongiform encephalopathy (BSE). Depending on the number of octapeptide repeat units present in the Prnp gene, the position of the SNP is either nucleotide 631 of exon 3 (codon 211) when the Prnp gene comprises six octapeptide repeat region sequences, nucleotide 607 of exon 3 (codon 203) when the Prnp gene comprises five octapeptide repeat region sequences, or nucleotide 655 of exon 3 (codon 219) when the Prnp gene comprises seven octapeptide repeat region sequences. Alleles of the bovine Prnp wherein the SNP at these positions is lysine (K) at the corresponding amino acids (i.e., 211, 203 or 219) in the bovine prion protein are all indicative of increased susceptibility to BSE in comparison to alleles which encode glutamic acid (E) at the same position. This SNP may be used as a marker for selecting bovines susceptible to BSE for disposal and / or removal from breeding, the human food and animal feed supplies.

The invention discloses new use of cell culture medium additive for substituting serum by sericin and a cell culture medium containing sericin to substitute serum; the cell culture medium disclosed by The invention comprises a basic culture medium and nutritional additive; the nutritional additive is 20-2000mug / ml of sericin; in traditional cell cultivation, bovine serum is added normally; but most of the bovine serum is imported and has high price; mass stability between batches is poor; high-temperature sterilization cannot be processed; serious virus such as mycoplasma, bovine spongiform encephalopathy and the like may be contained; and the bovine serum has significant risks to the cell cultivation. According to The invention, the serum is substituted by the sericin; cost is reduced greatly, stability of a cell cultivation system is enhanced, and pollution caused by serum is avoided; in addition, the cell cultivation medium additive disclosed by The invention has significant application value.

Proteins expressed from within the prion protein genes of all animals and humans, “prionins”, against which reagents can be prepared for accurate pre-symptomatic diagnosis, for detecting latent TSE, for detecting TSE contamination of food, blood and blood products and for therapeutic treatment of Bovine spongiform encephalopathy (BSE) in cows, Scrapie disease in sheep and Creutzfeldt-Jacob syndrome in humans, are revealed.

The present invention relates to a method for preparing a bone graft substitute using bovine bone, and more particularly to a method for preparing a safe bone graft substitute which does not have the risk of infection with bovine spongiform encephalopathy, the method comprising treating bovine bone with sodium hypochlorite and treating the treated bone at a high temperature of more than 600° C. The bone graft substitute does not cause an immune response, because it is prepared by effectively removing lipids and organic substances from bovine bone having a structure very similar to that of the human bone. Also, it has excellent osteoconductivity, and is free of prion, and thus it does not have the risk of infection with bovine spongiform encephalopathy. According to the disclosed invention, the bone graft substitute having such advantages can be prepared in a simple manner.

The present invention discloses a preparation method for prion protein gene knockout domestic animals. The process is characterized by: knocking off the prion protein gene of domestic animals on a cellular level; and preparing prion protein gene knockout domestic animals through somatic cell cloning method. The function of the prion protein of domestic animals is inactivated. The functional prion protein is not expressed, thus the domestic animals can resist to relative disease of prion protein, such as scrapie, bovine spongiform encephalopathy (mad cow disease) and the like.

The invention provides an orally disintegrating preparation. The orally disintegrating preparation comprises treatment medicines and auxiliary materials, wherein the auxiliary materials comprise collagen peptide and sugar alcohol, the treatment medicines account for 3%-20% of the total weight, the collagen peptide accounts for 2%-18% of the total weight, and the sugar alcohol accounts for 15%-80% of the total weight. The orally disintegrating preparation aims to solve the problem that medicines are difficult to swallow by ALS patients, children, old people and the like, meanwhile, a conventional auxiliary material, namely, gelatin, of the orally disintegrating preparation is abandoned, and the BSE (bovine spongiform encephalopathy) virus danger and the heavy metal chromium problem caused by the gelatin arouse wide concern.

The present invention provides a method of detecting abnormal serum nucleic acid profiles to assess the risk of a transmissible spongiform encephalopathy, e.g., BSE.

The present invention provides cloned transgenic ungulates (eg, cattle) in which the activity of a prion protein is reduced by one or more genetically engineered mutations. Desirably, these transgenic cattle are also genetically modified to express exogenous (eg, human) antibodies. These cattle are a safer source of human antibodies for medicinal purposes and a safer source of agricultural products due to their protection against prion-related diseases such as bovine spongiform encephalopathy (also known as mad cow disease).

A family of PCR assays is disclosed for determining, both qualitatively and quantitatively, presence of material from a predetermined species source and for quantifying the amount of such material. The assays are based respectively on SINEs uniquely characteristic of pig species, cow species, chicken species, and ruminant sub-order, and having a high copy number. The assays disclosed permit rapid, inexpensive evaluation of meat samples to facilitate elimination from their diet of pork or beef by persons desiring to avoid such food sources; as well as the assay of cattle feed to determine presence therein of ruminant-source proteins, which are a potential source of bovine spongiform encephalopathy (BSE), commonly referred to as “mad cow disease.” The assays amplify the predetermined unique SINEs and the resulting amplified mixture is then evaluated qualitatively by electrophoresis on gel containing ethidium bromide or quantitatively by SYBR Green-based detection or TaqMan chemistry. The invention also extends to kits, primers, and other products used in connection with the assays. The amplicons are selected to be from about 100 to 170 bp long.