Characterization of recombinant human epidermal growth factor produced in yeast

Carlos George-Nascimento, Alexander Gyenes, S. Mitchell Halloran, James Merryweather, Pablo Valenzuela, Kathelyn S. Steimer, Frank R. Masiarz, Anne Randolph

Resultado de la investigación: Article

67 Citas (Scopus)

Resumen

Four different forms of human epidermal growth factor (h-EGF) are found in the culture medium of a recombinant strain of Saccharomyces cerevisiae. These forms were characterized after purification using reverse-phase high-performance liquid chromatography. The most abundant form of secreted recombinant h-EGF has leucine at the carboxyl terminus and is identical with γ-urogastrone. A second species is identical with the most abundant form except that it lacks the carboxyl-terminal leucine. This form appears to be the product of a carboxypeptidase found in the growth medium. The other two forms of recombinant h-EGF are the respective oxidation products of the above where the single methionine residue has been converted to methionine sulfoxide. These four forms of recombinant h-EGF are fully active; they bind to the EGF receptor of A431 cells as well as stimulate mitotic activity of human foreskin fibroblasts with equal specific activity. The location of the disulfide bonds in the predominant form of recombinant h-EGF was determined following digestion with thermolysin. The amino acid compositions of the resulting peptides showed that the placement of disulfide bonds in recombinant h-EGF is identical with that in murine EGF.

Idioma originalEnglish
Páginas (desde-hasta)797-802
Número de páginas6
PublicaciónBiochemistry
Volumen27
N.º2
EstadoPublished - 1988

Huella dactilar

Epidermal Growth Factor
Yeast
Yeasts
Leucine
Disulfides
Thermolysin
Foreskin
Carboxypeptidases
High performance liquid chromatography
Reverse-Phase Chromatography
Fibroblasts
Epidermal Growth Factor Receptor
Human Activities
Methionine
Purification
Saccharomyces cerevisiae
Culture Media
Digestion
High Pressure Liquid Chromatography
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Citar esto

George-Nascimento, C., Gyenes, A., Halloran, S. M., Merryweather, J., Valenzuela, P., Steimer, K. S., ... Randolph, A. (1988). Characterization of recombinant human epidermal growth factor produced in yeast. Biochemistry, 27(2), 797-802.
George-Nascimento, Carlos ; Gyenes, Alexander ; Halloran, S. Mitchell ; Merryweather, James ; Valenzuela, Pablo ; Steimer, Kathelyn S. ; Masiarz, Frank R. ; Randolph, Anne. / Characterization of recombinant human epidermal growth factor produced in yeast. En: Biochemistry. 1988 ; Vol. 27, N.º 2. pp. 797-802.
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abstract = "Four different forms of human epidermal growth factor (h-EGF) are found in the culture medium of a recombinant strain of Saccharomyces cerevisiae. These forms were characterized after purification using reverse-phase high-performance liquid chromatography. The most abundant form of secreted recombinant h-EGF has leucine at the carboxyl terminus and is identical with γ-urogastrone. A second species is identical with the most abundant form except that it lacks the carboxyl-terminal leucine. This form appears to be the product of a carboxypeptidase found in the growth medium. The other two forms of recombinant h-EGF are the respective oxidation products of the above where the single methionine residue has been converted to methionine sulfoxide. These four forms of recombinant h-EGF are fully active; they bind to the EGF receptor of A431 cells as well as stimulate mitotic activity of human foreskin fibroblasts with equal specific activity. The location of the disulfide bonds in the predominant form of recombinant h-EGF was determined following digestion with thermolysin. The amino acid compositions of the resulting peptides showed that the placement of disulfide bonds in recombinant h-EGF is identical with that in murine EGF.",
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George-Nascimento, C, Gyenes, A, Halloran, SM, Merryweather, J, Valenzuela, P, Steimer, KS, Masiarz, FR & Randolph, A 1988, 'Characterization of recombinant human epidermal growth factor produced in yeast', Biochemistry, vol. 27, n.º 2, pp. 797-802.

Characterization of recombinant human epidermal growth factor produced in yeast. / George-Nascimento, Carlos; Gyenes, Alexander; Halloran, S. Mitchell; Merryweather, James; Valenzuela, Pablo; Steimer, Kathelyn S.; Masiarz, Frank R.; Randolph, Anne.

En: Biochemistry, Vol. 27, N.º 2, 1988, p. 797-802.

Resultado de la investigación: Article

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AU - George-Nascimento, Carlos

AU - Gyenes, Alexander

AU - Halloran, S. Mitchell

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AU - Valenzuela, Pablo

AU - Steimer, Kathelyn S.

AU - Masiarz, Frank R.

AU - Randolph, Anne

PY - 1988

Y1 - 1988

N2 - Four different forms of human epidermal growth factor (h-EGF) are found in the culture medium of a recombinant strain of Saccharomyces cerevisiae. These forms were characterized after purification using reverse-phase high-performance liquid chromatography. The most abundant form of secreted recombinant h-EGF has leucine at the carboxyl terminus and is identical with γ-urogastrone. A second species is identical with the most abundant form except that it lacks the carboxyl-terminal leucine. This form appears to be the product of a carboxypeptidase found in the growth medium. The other two forms of recombinant h-EGF are the respective oxidation products of the above where the single methionine residue has been converted to methionine sulfoxide. These four forms of recombinant h-EGF are fully active; they bind to the EGF receptor of A431 cells as well as stimulate mitotic activity of human foreskin fibroblasts with equal specific activity. The location of the disulfide bonds in the predominant form of recombinant h-EGF was determined following digestion with thermolysin. The amino acid compositions of the resulting peptides showed that the placement of disulfide bonds in recombinant h-EGF is identical with that in murine EGF.

AB - Four different forms of human epidermal growth factor (h-EGF) are found in the culture medium of a recombinant strain of Saccharomyces cerevisiae. These forms were characterized after purification using reverse-phase high-performance liquid chromatography. The most abundant form of secreted recombinant h-EGF has leucine at the carboxyl terminus and is identical with γ-urogastrone. A second species is identical with the most abundant form except that it lacks the carboxyl-terminal leucine. This form appears to be the product of a carboxypeptidase found in the growth medium. The other two forms of recombinant h-EGF are the respective oxidation products of the above where the single methionine residue has been converted to methionine sulfoxide. These four forms of recombinant h-EGF are fully active; they bind to the EGF receptor of A431 cells as well as stimulate mitotic activity of human foreskin fibroblasts with equal specific activity. The location of the disulfide bonds in the predominant form of recombinant h-EGF was determined following digestion with thermolysin. The amino acid compositions of the resulting peptides showed that the placement of disulfide bonds in recombinant h-EGF is identical with that in murine EGF.

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George-Nascimento C, Gyenes A, Halloran SM, Merryweather J, Valenzuela P, Steimer KS y otros. Characterization of recombinant human epidermal growth factor produced in yeast. Biochemistry. 1988;27(2):797-802.