Method for preparing fusion protein contg. human interferon-alpha 2 and human seralbumin and its products

A human serum albumin, fusion protein technology, applied in the field of long-acting fusion protein drugs, can solve the problems of increasing patient pain, treatment costs, toxic side effects, and high plasma clearance rate
CN1831124AInactive Publication Date: 2006-09-13JIANGNAN UNIV
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Patent Information

Authority / Receiving Office
CN · China
Current Assignee / Owner
JIANGNAN UNIV
Publication Date
2006-09-13
Estimated Expiration
Not applicable · inactive patent

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Abstract

The invention relates to a manufacture method and product for confluence albumen of human alpha-2 interferon and human serum albumin that uses superposing PCR technology, connecting IFN alpha-2 cDNA and HAS cDNA, with out any connecting peptide to gain IFN alpha-2 HSA cDNA melting gene to be integrated into host chromosome to take expression. The confluence albumen includes the first area of at least 85% sequence same source as human beta-interferon and the second area of at least 85% sequence of same source of human serum albumin. The invention has good application prospect in medicine field.
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Description

technical field

[0001] The preparation method and product of the fusion protein of human alpha 2 interferon and human serum albumin belong to the technical field of long-acting fusion protein medicine. Background technique

[0002] Human serum albumin (Human serum albumin, HSA) is the main protein component in plasma, and the concentration in plasma is 40mg / ml (Phillip P.Minghettis et al., THE JOURNAL OFBIOLOGICAL CHEMISTRY, 1986 261:6747-6757), In addition to its function of maintaining plasma osmotic pressure, it can also bind endogenous and / or exogenous ligands, including hormones, toxic metabolites, drugs, etc. By binding these ligands, HSA can regulate hormone activity, toxicity of endogenous and exogenous substances, and availability of drugs (Ji-Sook Ha et al., Biochimica et Biophysica Acta, 20031640: 119-128). The Half HSA constructed by David S. Park et al. (truncating the first 297 amino acid residues of HSA) has a secondary structure similar to the corresponding ...

Claims

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