Purification and characterization of protein disulphide-isomerase from the unicellular green alga Chlamydomonas reinhardii. A 120 kDa dimer antigenically distinct from the vertebrate enzyme

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Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C.Biochemical and biophysical characterization of a novel plant protein disulfide isomerase

P2860

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P2860

Purification and characterization of protein disulphide-isomerase from the unicellular green alga Chlamydomonas reinhardii. A 120 kDa dimer antigenically distinct from the vertebrate enzyme

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http://www.wikidata.org/entity/Q42794184

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1990 nî lūn-bûn

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1990年の論文

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1990年論文

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1990年論文

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1990年論文

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1990年論文

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1990年論文

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1990年论文

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1990年论文

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1990年论文

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Purification and characterizat ...... nct from the vertebrate enzyme

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Purification and characterizat ...... nct from the vertebrate enzyme

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Purification and characterizat ...... nct from the vertebrate enzyme

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Purification and characterizat ...... nct from the vertebrate enzyme

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Purification and characterizat ...... nct from the vertebrate enzyme

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Purification and characterizat ...... nct from the vertebrate enzyme

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Purification and characterizat ...... nct from the vertebrate enzyme

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Kaska DD

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Kivirikko KI

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Myllylä R

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P2860

Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase

The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum

A C-terminal signal prevents secretion of luminal ER proteins

Enzymically catalyzed disulfide interchange in randomly cross-linked soybean trypsin inhibitor.

Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit.

Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER.

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scholarly article

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10.1042/BJ2680063

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English

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268

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Purification and characterization of protein disulphide-isomerase from the unicellular green alga Chlamydomonas reinhardii. A 120 kDa dimer antigenically distinct from the vertebrate enzyme

about

P2860

P2860

Purification and characterization of protein disulphide-isomerase from the unicellular green alga Chlamydomonas reinhardii. A 120 kDa dimer antigenically distinct from the vertebrate enzyme

description

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P1433

P1476

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P2860

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P356

P407

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P698

P932