Abstract:
The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by purified aminopeptidase from Saccobolus platensis was investigated using the model heptapeptide L-R-R-A-S-L-G. Phosphorylation of serine greatly altered the action of peptidase producing a fragment, A-S(P)-L-G, insensitive to further attack by the peptidase. The action of peptidase was tested on peptides generated by subtilisin digestion of fungal cytosolic proteins labeled in vivo with [3H]leucine and phosphorylated in vitro with the catalytic subunit of cyclic AMP-dependent protein kinase. Phosphopeptides were enriched by gel filtration through P-2 columns. After exhaustive exopeptidase degradation the peak of [32p]phosphopeptides remained mostly unchanged. Removal of phosphate with alkaline phosphatase prior to treatment with peptidase produced a 12% liberation of [3H]leucine. The results support the idea that phosphorylation influences final protein processing. © 1994, Academic Press, Inc.. All rights reserved.
Registro:
Documento: |
Artículo
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Título: | Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action |
Autor: | Murray, P.F.; Passeron, S. |
Filiación: | Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, 4° Piso, Pabellón II, Buenos Aires, 1428, Argentina
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Palabras clave: | aminopeptidase; cyclic AMP-dependent protein kinase; dithiothreitol; DTT; kemptide; L-R-R-A-S-L-G; peptide processing; phosphopeptides; phosphorylation; PK A; proteolysis; aminopeptidase; cyclic AMP dependent protein kinase; heptapeptide; leucine; serine; subtilisin; tritium; article; cytosol; enzyme activity; fungus; gel filtration; nonhuman; priority journal; protein degradation; protein phosphorylation; Fungi; Saccobolus; Tritium |
Año: | 1994
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Volumen: | 18
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Número: | 4
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Página de inicio: | 320
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Página de fin: | 329
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DOI: |
http://dx.doi.org/10.1016/S0147-5975(06)80005-8 |
Título revista: | Experimental Mycology
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Título revista abreviado: | Exp. Mycol.
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ISSN: | 01475975
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CAS: | aminopeptidase, 9031-94-1; cyclic AMP dependent protein kinase; leucine, 61-90-5, 7005-03-0; serine, 56-45-1, 6898-95-9; subtilisin, 9014-01-1; tritium, 10028-17-8
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Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v18_n4_p320_Murray |
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Citas:
---------- APA ----------
Murray, P.F. & Passeron, S.
(1994)
. Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action. Experimental Mycology, 18(4), 320-329.
http://dx.doi.org/10.1016/S0147-5975(06)80005-8---------- CHICAGO ----------
Murray, P.F., Passeron, S.
"Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action"
. Experimental Mycology 18, no. 4
(1994) : 320-329.
http://dx.doi.org/10.1016/S0147-5975(06)80005-8---------- MLA ----------
Murray, P.F., Passeron, S.
"Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action"
. Experimental Mycology, vol. 18, no. 4, 1994, pp. 320-329.
http://dx.doi.org/10.1016/S0147-5975(06)80005-8---------- VANCOUVER ----------
Murray, P.F., Passeron, S. Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action. Exp. Mycol. 1994;18(4):320-329.
http://dx.doi.org/10.1016/S0147-5975(06)80005-8