87 results about "Human Parathyroid" patented technology

Disclosed are an antibody against human para-thyroid-hormone-related protein, a DNA coding for the antibody, a recombinant vector containing the DNA, a transformant transformed with the recombinant vector, a method for preparation of the antibody, and uses of the antibody.

Synthetic and/or recombinant biologically active peptide derivatives of PTH(1-28), comprising a biologically active peptide at least 90% identical to a peptide consisting essentially of the formula:

(b) fragments thereof containing amino acids 1-24, 1-25, 1-26, or 1-27; (c) pharmaceutically acceptable salts thereof; or (d) N- or C-derivatives thereof; wherein:

• • • X₀₁ is Ser, Ala or Gly; and
    • X₀₂ is Glu or Arg,

provided that said peptide is not hPTH(1-26)NH₂, hPTH(1-27)NH₂ or hPTH(1-28)NH₂.

The invention discloses fluorescence immunochromatography test paper for achieving intraoperative judgment of parathyroid tissues through quantitatively detecting a human parathyroid hormone (PTH) and a preparation method of the fluorescence immunochromatography test paper. The test paper capable of detecting the human PTH through a double-antibody sandwich method and a fluorescence immunochromatography; the antibody is prepared by using a specific antigen peptide. The human PTH in a to-be-detected matter can be quickly and accurately detected, so that the fluorescence immunochromatography test paper is simple, convenient and fast to operate, wide in detection range, high in specificity and good in sensitivity.

The present invention relates to pharmaceutical formulations comprising human parathyroid hormone at a concentration from 0.3 to 10 mg/ml, a pharmaceutically acceptable buffer having a pH from 4 to 6, and at least one tonicity modifier. The said pharmaceutical formulations are useful for the treatment of bone related disorders such as osteoporosis.

A human parathyroxni 1-34 peptide associated peptide Pro-Pro-[Arg11]hPTH(1-34)-Pro-Pro. It is a precursor peptide, whose two terminal Proscan be excised in human body to become bioactive [Arg11]hPTH(1-34)-Pro-Pro. Its preparing process includes such steps as culturing the host cell of pED-4P-[Arg11]hPTH(1-34), separating the fusion protein of Pro-Pro-[Arg11]hPTH(1-34)-Pro-Pro from the cultured substance, and excising two Pros by dipeptidase in body to obtain [Arg11]hPTH(1-34)-Pro-Pro.

The present invention relates to a preparation process of recombinant human parathyroid hormone PTH(1-34). The process constitutes a new engineering strain to result in high expression amount, simplepurifying course and low cost.The present invention adopts colibacillus degenerate codon modifying sequence corresponding cDNA, the basic sequence is L-V-P-R-PTH(1-34), where L-V-P-R is the enzyme incision site of thrombin. To the end of the nucleotides sequence, colibacillus terminator codon TAA is added; and in order to clone easily to the 5'-terminal enzyme incision site of EcoR I is added, and to the 3'-terminal, enzyme incision site of Sal I is added. High-purity recombinant huamn parathyroid hormone PTH(1-34) is obtained through fermentation of the engineering bacteria, occlusion body extraction, diluting renaturation, thrombase incision, anionic exchange chromatography and other steps.

The invention discloses a preparing method of the recombination human parathyroid hormone 1-84 by the gene engineering technology. It uses the codon for E.Coli and synthesizes the encoding sequence of the rhPTH1-84 and constructs the carrier and engineering bacteria. The invention is to express the soluble fusion protein contain the whole sequence of the hPTh 1-84 in the E.Coli cytoplasm, then the protein is purified by the chelate chromatography and cut by the enterokinase, next to purify by the ionic exchange and the gel chromatography to get the rhPTH 1-84 which the purity is more than 80%, the yield can reach 300mg/L.

A medical component comprising a human parathyroid hormone peptide or its derivative, and acetic acid contained at a concentration less than its chemical equivalent with respect to the human parathyroid hormone peptide or to its derivative. Since in the medical component acetic acid, which is present as a salt of or attached to the peptide or its derivative, has been reduced to an amount less than chemical equivalent with respect to the human parathyroid hormone peptide or its derivative, a medical component, which is highly stable and will ensure an excellent use feeling when introduced into a pharmaceutical composition, is obtained.

The invention discloses a fusion protein of human sperm albumin and human parathyroid hormone (1-34), and DNA sequence coding it as well as bacteria, yeast, animal cells and plant cells that carry the DNA sequence. It contains a first region with at least 85% sequence isogeny with human sperm albumin and a second region with at least 85% sequence isogeny with hPTH (1-34), and can substitute, delete or add several aminophenol residues on the premise of not changing its own property; there is a peptide linkage between the two regions; it not only retains the functional actions of hPTH (1-34) to activate receptor and stimulate bon reconstruction but also remarkably prolongs in vivo half life, and it is a medicinal protein that can cure osteoporosis.

The invention provides a method for preparing human serum albumin-human parathyroid hormone. By means of transforming a yeast host SMD1168, yapson1 coded sequences on the SMD 1168 can be knocked out. On the basis of the SMD 1168, coded gene YPS1 of yapson1 is further knocked out, namely double knockouts of a proteinase A and yapsin1 are achieved, and the transformed host is named as SMD1168yps1 delta. By the aid of the transformed host, a recombination expression of fusion proteins of human serum albumin-human parathyroid hormone (1-34) is optimized, so that the degradation of interest proteins in the expressing process can be reduced, and downstream mass production costs and difficulties of separation and purification are lowered. According to the method, the optimized the human serum albumin-human parathyroid hormone (1-34) fusion proteins can be applied to prepare parathyroid hormone (PTH) (1-34) medicines which are used for treating osteoporosis.

The present invention relates to a method for monitoring effects of administration of a parathyroid hormone by determining levels of one or more markers of an activity of this hormone. Suitable markers of bone formation include one or more enzymes indicative of osteoblastic processes of bone formation, preferably bone specific alkaline phosphatase, and/or one or more products of collagen biosynthesis, preferably a procollagen I C-terminal propetide. Suitable markers of bone resorption and turnover include one or more products of collagen degradation, preferably an N-terminal telopeptide (NTX). In addition, methods for concurrently reducing the risk of both vertebral and non-vertebral bone fracture in a male human subject at risk of or having ossteoporosis are also disclosed, involving administration of human parathyroid hormone (amino acid sequence 1-34) without concurrent administration of an antiseropositive agent other than vitamin D or calcium.

The invention relates to the technical field of biomedical engineering, and relates to a method for preparing human parathyroid hormone (1-34) through fermenting and purifying human parathyroid hormone 1-34 recombinant engineering bacteria constructed by a gene engineering method. The method provided by the invention comprises the following steps: fusing and expressing the genes for coding human parathyroid hormone and a thioredoxin label, and further constructing and finishing genetic engineering bacteria capable of highly expressing human parathyroid hormone; adding IPTG (isopropyl beta D thiogalactopy ranoside) and triton X-100 in the fermentation process by adopting a chemosmosis fermentation technology so as to improve the release of proteins extracellularly in the fermentation process, which is good for the continuous synthesis of proteins, and avoiding the attack of endoproteinase, thus protein high-yield extracellular accumulation is promoted; and simultaneously carrying out heat treatment on a fermentation liquid when the fermentation reaches the final point aiming at the heat stability of thioredoxin fusion, thus initially purified target proteins are directly recycled and obtained from a fermentation liquor supernatant after centrifugation.

This invention provides a method for preparing recombinant human parathyroid hormone 1-34 (rhPTH (1-34)). The method comprised: (1) expressing with an expression vector capable of expressing a fusion protein with an amino acid sequence (from N-terminal to C-terminal) containing thioredoxin, (His) 6, enterokinase recognition site and parathyroid hormone 1-34 peptide; (2) purifying the fusion protein by nickel ion complexation affinity chromatography; (3) cutting the purified fusion protein with enterokinase to release the rhPTH (1-34) from the fusion protein. By this method, rhPTH (1-34) can be purified rapidly, simply and efficiently, and the recovery yield is largely increased.

The present invention provides a kind of fusion protein, which possesses thioredoxin sequence and parathormone peptide 1-34 located in the downstream of the thioredoxin. Preferably, the fusion protein possesses also connecting peptide containing proteolytic enzyme recognizing site and located between the thioredoxin and the parathormone peptide 1-34. From the fusion protein, human parathormone peptide 1-34 may be prepared.

The invention discloses a method for rapidly identifying human parathyroid glands. The method is realized by using parathyroid hormone (PTH) fluorescence immunochromatography test paper to determine the content of PTH in liquid to be detected; the test paper is used for detecting human PTH by using a double-antibody sandwich method and a fluorescence immunochromatography; the antibodies are prepared by using specific antigenic epitope peptide. The method can be used for accurately detecting the human PTH in a matter to be detected, and is simple and convenient to operate, wide in detection range, high in specificity and good in sensitivity.

The present invention relates to a novel method for purifying teriparatide, a therapeutically active polypeptide fragment of full-length human parathyroid hormone. The method is based on ion exchange chromatography and is effective in separating the therapeutically active polypeptide from undesirable variants, such as truncated polypeptides. The method of the invention can be used at a preparative scale which allows it to be implemented into the production process for teriparatide. Accordingly, the invention also provides a method for the production of teriparatide which includes a step in which teriparatide is purified by the novel ion exchange chromatography method of the invention.

The invention relates to a method for purifying human parathyroid hormone (1 to 34). The invention provides a method suitable to industrially purify lepirudin, which comprises the following steps: (1) using octadecylsilane chemically bonded silica as a solid phase, using a phosphate buffered solution the pH value of which is between 2.5 and 3.5 as an A phase, using acetonitrile as a B phase and carrying out gradient elution on crude peptide solution, wherein the gradient B percent is between 17 and 32 percent; (2) and adopting the reversed phase high performance liquid chromatography to convert lepirudin into acetate. The method for purifying lepirudin, which is provided by the invention, has simple operation, high product purity and good yield and reaches the industrialization requirements.

The present invention discloses a process for the preparation of rhPTH (1-34) also known as teriparatide by con-struction of a novel nucleotide, as an NcoI.IXhoI fragemt as set forth in SEQ. ID. No.:1 encoding a chimeric fusion protein as set forth in SEQ.ID. No.:2 comprising of a fusion partner consisting of 41 amino acids belonging to Escherichia coli β-galactosidase (LacZ) gene, an endopeptidase cleavage site, rhPTH (1-34) gene fragment, cloning the said nucleotide in an expression vector under the control of T7 promoter, transforming Escherichia coli with the said vector and expressing the chimeric fusion protein in fed batch fermentation. The present invention further discloses a low feed rate lactose induction for optimized expression of rhPTH (1-34) in Escherichia coli. The present invention also discloses an unique, novel two step orthogonal purification process for rhPTH (1-34) comprising of cation exchange chromatography optionally followed by preparative chromatography selected from HIC or RP-HPLC to yield a target protein of ≧99% purity. The present invention discloses a simple, cost-effective, environmentally benign method of producing high purity rhPTH (1-34).