Expression of recombinant pro-neuropeptide Y, proopiomelanocortin, and proenkephalin: relative processing by ‘prohormone thiol protease’ (PTP)

Autor: Liane M. Mende-Mueller, Martin R. Schiller, Vivian Hook, Andrea B. Kohn, Kurt W. Miller
Rok vydání: 1996
Předmět:
endocrine system
Pro-Opiomelanocortin
animal structures
Swine
Recombinant Fusion Proteins
Molecular Sequence Data
Prohormone
Biophysics
Prohormone convertase
Biology
environment and public health
Biochemistry
Substrate Specificity
law.invention
03 medical and health sciences
0302 clinical medicine
Proopiomelanocortin
Structural Biology
law
Escherichia coli
Genetics
medicine
Animals
Neuropeptide Y
Amino Acid Sequence
Protein Precursors
Molecular Biology
030304 developmental biology
0303 health sciences
Base Sequence
Enkephalins
Cell Biology
Neuropeptide Y receptor
Cysteine protease
Molecular biology
Proprotein processing
Rats
Proenkephalin
Cysteine Endopeptidases
enzymes and coenzymes (carbohydrates)
biology.protein
Recombinant DNA
Proprotein Convertases
Recombinant prohormone
Protein Processing
Post-Translational
030217 neurology & neurosurgery
medicine.drug
Zdroj: FEBS Letters. 382:6-10
ISSN: 0014-5793
DOI: 10.1016/0014-5793(96)00083-x
Popis: The preference of the ‘prohormone thiol protease’ (PTP), a candidate prohormone processing enzyme, for different peptide precursors was assessed in vitro with recombinant prohormones near estimated in vivo levels. Pro-neuropeptide Y (pro-NPY), prooplomelanocortin (POMC), and proenkephalin (PE) were expressed at high levels in E. coli. Purification of prohormones utilized a combination of DEAE-Sepharose, Mono Q, and preparative electrophoresis. PTP cleaved PE most readily, and also cleaved pro-NPY. The processing of POMC by PTP was minimal. These results demonstrate PTP's preference for certain prohormone substrates.
Databáze: OpenAIRE
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