Literature DB >> 446864

Resolution of ox liver thiol-disulphide oxidoreductases by a new application of covalent chromatography.

D A Hillson, R B Freedman.   

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Year:  1979        PMID： 446864     DOI： 10.1042/bst0070573

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN： 0300-5127            Impact factor:   5.407


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  5 in total

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

Authors:  D D Kaska; K I Kivirikko; R Myllylä
Journal:  Biochem J       Date:  1990-05-15       Impact factor: 3.857

2.  Molecular cloning of a multifunctional chicken protein acting as the prolyl 4-hydroxylase beta-subunit, protein disulphide-isomerase and a cellular thyroid-hormone-binding protein. Comparison of cDNA-deduced amino acid sequences with those in other species.

Authors:  T Parkkonen; K I Kivirikko; T Pihlajaniemi
Journal:  Biochem J       Date:  1988-12-15       Impact factor: 3.857

3.  Bovine liver thiol-protein disulphide oxidoreductases. An alternative method for differential purification and resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase.

Authors:  D A Hillson; R B Freedman
Journal:  Biochem J       Date:  1980-11-01       Impact factor: 3.857

4.  Resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase activities by covalent chromatography.

Authors:  D A Hillson; R B Freedman
Journal:  Biochem J       Date:  1980-11-01       Impact factor: 3.857

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

Authors:  T Pihlajaniemi; T Helaakoski; K Tasanen; R Myllylä; M L Huhtala; J Koivu; K I Kivirikko
Journal:  EMBO J       Date:  1987-03       Impact factor: 11.598
  5 in total

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