rhEPO (recombinant human eosinophil peroxidase): expression in Pichia pastoris and biochemical characterization

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Glycosylation characterization of recombinant human erythropoietin produced in glycoengineered Pichia pastoris by mass spectrometry.

P2860

Q35066979-2AF7BDDA-8D0E-44E1-8256-6AF28CE0F9F2

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rhEPO (recombinant human eosinophil peroxidase): expression in Pichia pastoris and biochemical characterization

Item

http://www.wikidata.org/entity/Q42037514

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

2006年论文

@zh

2006年论文

@zh-cn

name

rhEPO (recombinant human eosin ...... d biochemical characterization

@en

rhEPO

@nl

type

Item

label

rhEPO (recombinant human eosin ...... d biochemical characterization

@en

rhEPO

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rhEPO (recombinant human eosin ...... d biochemical characterization

@en

rhEPO

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rhEPO (recombinant human eosin ...... d biochemical characterization

@en

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Alessandra Gambacurta

http://www.w3.org/2001/XMLSchema#string

Chiara Ciaccio

http://www.w3.org/2001/XMLSchema#string

Christina Sakarikou

http://www.w3.org/2001/XMLSchema#string

Domenico Spagnolo

http://www.w3.org/2001/XMLSchema#string

Giampiero De Sanctis

http://www.w3.org/2001/XMLSchema#string

Giovanni Petrella

http://www.w3.org/2001/XMLSchema#string

Massimo Coletta

http://www.w3.org/2001/XMLSchema#string

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Substrates and products of eosinophil peroxidase

"Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A

Eosinophils preferentially use bromide to generate halogenating agents

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis

Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris.

Glycosylation of Pichia pastoris-derived proteins.

Heterologous protein expression in the methylotrophic yeast Pichia pastoris.

Mechanisms of eosinophil-associated inflammation.

Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity.

Human eosinophil peroxidase: purification and characterization.

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295-301

http://www.w3.org/2001/XMLSchema#string

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scholarly article

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10.1042/BJ20051385

http://www.w3.org/2001/XMLSchema#string

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English

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http://www.w3.org/2001/XMLSchema#string

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395

http://www.w3.org/2001/XMLSchema#string

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2006-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

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16396635

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P932

1422775

http://www.w3.org/2001/XMLSchema#string

rhEPO (recombinant human eosinophil peroxidase): expression in Pichia pastoris and biochemical characterization

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P2860

P2860

rhEPO (recombinant human eosinophil peroxidase): expression in Pichia pastoris and biochemical characterization

description

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932