BIOMAT Database Logo BIOMAT Database Logo

Structure of recombinant human interleukin 5 produced by Chinese hamster ovary cells. 1990

Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Suntory Institute for Biomedical Research, Osaka.

The complete peptide map of purified recombinant human interleukin 5 (rhIL-5) was determined to verify its primary structure, glycosylation sites, and disulfide bonding structure. Each peptide fragment generated by Achromobacter protease I (API) digestion was purified and characterized by amino acid analysis and amino acid sequence analysis. After digestion with API, we could identify all the peptides which were expected from human IL-5 cDNA sequence. The analyses of sulfhydryl content in rhIL-5 molecule and disulfide-containing peptide obtained from API digestion indicated that active form of rhIL-5 existed as an antiparallel dimer linked by two pairs of Cys-44 and Cys-86. In addition, we concluded that Thr-3 and Asn-28 were glycosylated. The results indicate that primary structure of rhIL-5 is highly homogeneous and observed heterogeneity is due to the difference in the content of carbohydrate.

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
D010053 Ovary The reproductive organ (GONADS) in female animals. In vertebrates, the ovary contains two functional parts: the OVARIAN FOLLICLE for the production of female germ cells (OOGENESIS); and the endocrine cells (GRANULOSA CELLS; THECA CELLS; and LUTEAL CELLS) for the production of ESTROGENS and PROGESTERONE. Ovaries
D010449 Peptide Mapping Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases. Fingerprints, Peptide,Peptide Fingerprinting,Protein Fingerprinting,Fingerprints, Protein,Fingerprint, Peptide,Fingerprint, Protein,Fingerprinting, Peptide,Fingerprinting, Protein,Mapping, Peptide,Peptide Fingerprint,Peptide Fingerprints,Protein Fingerprint,Protein Fingerprints
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
D004220 Disulfides Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties. Disulfide
D005260 Female Females
D006031 Glycosylation The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION). Protein Glycosylation,Glycosylation, Protein
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
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Polypeptide and carbohydrate structure of recombinant human interleukin-6 produced in Chinese hamster ovary cells.
February 1994, Journal of biochemistry,
Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Purification and characterization of recombinant human interleukin 5 expressed in Chinese hamster ovary cells.
July 1989, Journal of biochemistry,
Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Characterization of recombinant human erythropoietin produced in Chinese hamster ovary cells.
May 1987, Biochemistry,
Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Characterization of recombinant murine interleukin 5 expressed in Chinese hamster ovary cells.
October 1992, Glycobiology,
Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Carbohydrate structures of human interleukin 5 expressed in Chinese hamster ovary cells.
November 1991, Journal of biochemistry,
Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Characterization of latent recombinant TGF-beta 2 produced by Chinese hamster ovary cells.
January 1991, Journal of cellular biochemistry,
Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Expression and purification of recombinant human angiopoietin-2 produced in Chinese hamster ovary cells.
February 2005, Protein expression and purification,
Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Expression and purification of recombinant human angiopoietin-1 produced in Chinese hamster ovary cells.
January 2007, In vitro cellular & developmental biology. Animal,
Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Characterization of recombinant human diamine oxidase (rhDAO) produced in Chinese Hamster Ovary (CHO) cells.
June 2016, Journal of biotechnology,
Y Minamitake, and S Kodama, and T Katayama, and H Adachi, and S Tanaka, and M Tsujimoto
Relationship between sugar chain structure and biological activity of recombinant human erythropoietin produced in Chinese hamster ovary cells.
October 1989, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!