JPS6451097A - Purification of fused protein - Google Patents

Purification of fused protein

Info

Publication number
JPS6451097A
JPS6451097A JP20861687A JP20861687A JPS6451097A JP S6451097 A JPS6451097 A JP S6451097A JP 20861687 A JP20861687 A JP 20861687A JP 20861687 A JP20861687 A JP 20861687A JP S6451097 A JPS6451097 A JP S6451097A
Authority
JP
Japan
Prior art keywords
protein
peptide
amino acid
acid sequence
fused protein
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Pending
Application number
JP20861687A
Other languages
Japanese (ja)
Inventor
Susumu Matsuda
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Toray Industries Inc
Original Assignee
Toray Industries Inc
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Toray Industries Inc filed Critical Toray Industries Inc
Priority to JP20861687A priority Critical patent/JPS6451097A/en
Publication of JPS6451097A publication Critical patent/JPS6451097A/en
Pending legal-status Critical Current

Links

Landscapes

  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Peptides Or Proteins (AREA)

Abstract

PURPOSE:To purify the titled compound effective for promoting insulin secretion industrially and advantageously, by bringing a fused protein obtained by bonding a peptide having a specific amino acid sequence to a protein having specific molecular weight in an clevable way into contact with an adsorbent of silica type and eluting. CONSTITUTION:A gene to code a fused protein obtained by bonding spittle peptide P-C having amino acid sequence shown by the formula, found in the spittle, to a protein (e.g. beta-D-galactosidase) having >=10,000 in an clevable way is prepared. The gene is linked to a manifestation vector and inserted into Escherichia coli, which is transformed. Then the transformed Escherichia coli is cultivated to give a supernatant liquid of culture containing a large amount of a protein comprising a peptide having the amino acid sequence shown by the formula. Further the supernatant liquid is passed through a column packed with a silica-based adsorbent, the eluate is made to flow and the adsorbed substance is eluted to give the aimed fused protein.
JP20861687A 1987-08-21 1987-08-21 Purification of fused protein Pending JPS6451097A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP20861687A JPS6451097A (en) 1987-08-21 1987-08-21 Purification of fused protein

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP20861687A JPS6451097A (en) 1987-08-21 1987-08-21 Purification of fused protein

Publications (1)

Publication Number Publication Date
JPS6451097A true JPS6451097A (en) 1989-02-27

Family

ID=16559173

Family Applications (1)

Application Number Title Priority Date Filing Date
JP20861687A Pending JPS6451097A (en) 1987-08-21 1987-08-21 Purification of fused protein

Country Status (1)

Country Link
JP (1) JPS6451097A (en)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5451660A (en) * 1993-12-13 1995-09-19 Genentech, Inc. Method for purifying polypeptides

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5451660A (en) * 1993-12-13 1995-09-19 Genentech, Inc. Method for purifying polypeptides

Similar Documents

Publication Publication Date Title
Sassenfeld et al. A polypeptide fusion designed for the purification of recombinant proteins
US5310663A (en) Affinity peptides
Takao et al. Primary structure of heat-stable enterotoxin produced by Yersinia enterocolitica
CA2124271A1 (en) Process for preparing and purifying alpha-interferon
IL68790A (en) Polydeoxyribonucleotide coding for ifn-alpha2(arg),plasmid containing it,cloning of said plasmid and microorganisms containing it and ifn-alpha(arg)encoded by said polydeoxyribonucleotide and its preparation
IL118201A (en) Preparation comprising a protein with human erythropoietin activity which is free of serum and non-recombinant mammalian protein and process for the preparation thereof
US4172071A (en) Chromophore blue adsorbent method for the purification of preparations having an interferon type activity
EP0215658A3 (en) Improved formulation for recombinant beta-interferon processes for recovery and stabilization of beta-interferon and the use thereof
CA2676074A1 (en) Chromatographic method for high yield purification and viral inactivation of antibodies
US4551271A (en) Purification of interferon by metal chelate chromatography
CA1133898A (en) Purification of interferon
CA2168459A1 (en) Fusion proteins containing the c-terminal of tetanus toxin linked to a heterologous protein
NZ203364A (en) Method for purifying human immune interferon;homogeneous human immune interferon
US5633350A (en) Method for the isolation and purification of vitamin K-dependent proteins
NO902251L (en) PREPARATION OF GONORIC P1 PROTEINS AND VACCINES.
JPS6451097A (en) Purification of fused protein
HK1006727A1 (en) Protein structure of the plant toxin gelonin
DE555135T1 (en) Process for the production of high purity fibrinogen, high purity fibrinogen thus obtained and pharmaceutical composition containing the same.
Scott et al. Purification of synexin by pH step elution from chromatofocusing media in the absence of ampholytes
Yamamoto et al. Highly efficient purification of the 33-, 24-, and 18-kDa proteins in spinach photosystem II by butanol/water phase partitioning and high-performance liquid chromatography
JPS6439990A (en) Fused gene by bonding aequorin gene to functional gene
Kobayashi et al. Putative ammo-terminal presequence for β-subunit of plant mitochondrial F1ATPase deduced from the amino-terminal sequence of the mature subunit
Lu et al. Isolation and Characterization of Human Tissue Kallikrein Produced inEscherichia coli: Biochemical Comparison to the Enzymatically Inactive Prokallikrein and Methionyl Kallikrein
Rock et al. Overexpression and structure-function analysis of a bioengineered IL-2/IL-6 chimeric lymphokine
JPH06800B2 (en) Purification method of human interferon-β