FEBS Letters | |
Purification and characterization of a novel tripeptidyl aminopeptidase from Streptomyces lividans 66 | |
Krieger, Timothy J.1  Bartfeld, Daniel1  Hadary, Dany1  Jenish, David L.1  | |
[1] Cangene Corporation, 6280 Northwest Drive, Mississauga, Ontario L4V 1J7, Canada | |
关键词: Tripeptidyl aminopeptidase; Recombinant protein expression; Protein degradation; Serine proteinase; Fermentation Streptomyces lividans; EPO; recombinant human erythropoeitin; GM-CSF; recombinant human granulocyte macrophage colony stimulating factor; IL-3; recombinant human interleukin-3; IL-6; recombinant human N-alanyl interleukin-6; PMSF; phenylmethanesulfonylfluoride; TAP; tripeptidyl aminopeptidase; | |
DOI : 10.1016/0014-5793(94)00988-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
An extracellular tripeptidyl aminopeptidase has been purified from Streptomyces lividans 66 cell-free cultures. The enzyme is a major component of the secreted proteolytic activity. The protease removes only the N-terminal tripeptide from recombinant human GM-CSF and IL-3 but does not cleave recombinant human IL-6. The enzyme cleaves the synthetic tripeptide substrates APA-pNA and APM-pNA but does not cleave substrates with blocked amino terminals. Smaller substrates are not cleaved. The enzyme appears to be a serine protease of 55 kDa molecular weight. The pH optimum is between 7.5 and 8.5 but varies slightly with the substrate. The N-terminal sequence and amino acid composition have been determined.
【 授权许可】
Unknown
【 预 览 】
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