BIOMAT Database Logo BIOMAT Database Logo

Production, purification and characterization of biologically active recombinant human nerve growth factor. 1990

M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Biotechnology Research Laboratories, Takeda Chemical Industries, Ltd., Osaka, Japan.

The human NGF gene was isolated and inserted downstream from murine leukemia virus LTR in a plasmid having dihydrofolate reductase cDNA. The expression plasmid was introduced into CHO cells. Selection of the transformants for the resistance to methotrexate gave a CHO cell line which produced human NGF at a level of 4 mg/L in the culture medium. The recombinant human NGF was purified to near homogeneity from the culture supernatant. The NH2-terminal amino acid sequence, the COOH-terminal amino acid (Ala), and the amino acid composition of the human NGF were identical to those deduced from the nucleotide sequence of the human NGF gene. The recombinant human NGF was composed of 120 amino acid residues. Three disulfide linkages were determined to be Cys15-Cys80, Cys-58-Cys108, and Cys68-Cys110; the locations were identical to those in the mouse 2.5S NGF molecule. The specific biological activity of the recombinant human NGF was comparable with that of authentic mouse 2.5S NGF as determined by stimulation of neurite outgrowth from PC12 cells.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009414 Nerve Growth Factors Factors which enhance the growth potentialities of sensory and sympathetic nerve cells. Neurite Outgrowth Factor,Neurite Outgrowth Factors,Neuronal Growth-Associated Protein,Neuronotrophic Factor,Neurotrophic Factor,Neurotrophic Factors,Neurotrophin,Neurotrophins,Growth-Associated Proteins, Neuronal,Neuronal Growth-Associated Proteins,Neuronotrophic Factors,Neurotrophic Protein,Neurotrophic Proteins,Proteins, Neuronal Growth-Associated,Factor, Neurite Outgrowth,Factor, Neuronotrophic,Factor, Neurotrophic,Factors, Nerve Growth,Factors, Neurite Outgrowth,Factors, Neuronotrophic,Factors, Neurotrophic,Growth Associated Proteins, Neuronal,Growth-Associated Protein, Neuronal,Neuronal Growth Associated Protein,Neuronal Growth Associated Proteins,Outgrowth Factor, Neurite,Outgrowth Factors, Neurite,Protein, Neuronal Growth-Associated
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D003412 Cricetulus A genus of the family Muridae consisting of eleven species. C. migratorius, the grey or Armenian hamster, and C. griseus, the Chinese hamster, are the two species used in biomedical research. Hamsters, Armenian,Hamsters, Chinese,Hamsters, Grey,Armenian Hamster,Armenian Hamsters,Chinese Hamster,Chinese Hamsters,Grey Hamster,Grey Hamsters,Hamster, Armenian,Hamster, Chinese,Hamster, Grey
D005822 Genetic Vectors DNA molecules capable of autonomous replication within a host cell and into which other DNA sequences can be inserted and thus amplified. Many are derived from PLASMIDS; BACTERIOPHAGES; or VIRUSES. They are used for transporting foreign genes into recipient cells. Genetic vectors possess a functional replicator site and contain GENETIC MARKERS to facilitate their selective recognition. Cloning Vectors,Shuttle Vectors,Vectors, Genetic,Cloning Vector,Genetic Vector,Shuttle Vector,Vector, Cloning,Vector, Genetic,Vector, Shuttle,Vectors, Cloning,Vectors, Shuttle
D006224 Cricetinae A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS. Cricetus,Hamsters,Hamster
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Production and characterization of biologically active recombinant human nerve growth factor.
January 1989, Neurobiology of aging,
M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Production and characterization of biologically active recombinant beta nerve growth factor.
January 1988, Molecular and cellular biology,
M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Production of biologically active recombinant human factor H in Physcomitrella.
April 2011, Plant biotechnology journal,
M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Purification and characterization of biologically active recombinant human Eppin expressed in Escherichia coli.
April 2008, Chinese medical journal,
M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Production and purification of biologically active recombinant tilapia (Oreochromis niloticus) prolactins.
November 1991, The Journal of endocrinology,
M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Biochemical characterization of recombinant human nerve growth factor.
November 1992, Journal of neurochemistry,
M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Yeast-derived recombinant human insulin-like growth factor I: production, purification, and structural characterization.
February 1990, Journal of protein chemistry,
M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Overproduction of biologically-active human nerve growth factor in Escherichia coli.
December 1992, Bioscience, biotechnology, and biochemistry,
M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Large-scale production of biologically active human keratinocyte growth factor-2.
March 2009, Applied microbiology and biotechnology,
M Iwane, and Y Kitamura, and Y Kaisho, and K Yoshimura, and A Shintani, and R Sasada, and S Nakagawa, and K Kawahara, and K Nakahama, and A Kakinuma
Growth-regulated synthesis and secretion of biologically active nerve growth factor by human keratinocytes.
November 1991, The Journal of biological chemistry,
Copied contents to your clipboard!