Structural Characterization of Fibroblast Human Interferon-β1
作者： KAZUO HOSOI , JUN UTSUMI , TEIZO KITAGAWA , HIROHIKO SHIMIZU , SIGEYASU KOBAYASHI
关键词: Nucleic acid sequence 、 Residue (chemistry) 、 Fibroblast 、 Complementary DNA 、 Sequence (biology) 、 Biology 、 Peptide 、 Biochemistry 、 Interferon 、 Peptide sequence
摘要: The complete amino acid sequence of fibroblast human interferon-β1 (IFN-β1) was determined, and the higher-order structure protein characterized with Raman spectroscope. That identical to entire deduced from cDNA nucleotide sequence, showing there are no proteolytic cleavages carboxyterminal residues in contrast natural IFN-α IFN-γ. N-glycosylation site confirmed as Asn-80 by detection glucosamines peptide containing Asn-80. An S-carboxymethyl Cys-17 detected S-carboxymethylated protein, suggesting that is unpaired. spectra indicated a predominance α-helical backbone three Cys this form, one unpaired residue disulfide bond. These results provide some evidence for primary structures IFN-β1 so far predicted.
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