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Literature summary for 5.3.4.1 extracted from

  • Hillson, D.A.; Freedman, R.B.
    Resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase activities by covalent chromatography (1980), Biochem. J., 191, 373-388.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.4.1

Inhibitors

Inhibitors Comment Organism Structure
Cd2+
-
 Bos taurus
iodoacetate
-
 Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km for scrambled ribonuclease: 0.023 mg/ml Bos taurus
0.0054
-
 dithiothreitol
-
 Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
 x * 57000, SDS-PAGE Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Proteins native, reduced or with wrong disulfide bonds Bos taurus Proteins with correct disulfide bonds ?
Proteins cosubstrate dithiothreitol can be replaced by GSH, cysteamine, 2-mercaptoethanol, thioglycollic acid or L-Cys, but at significantly higher concentrations Bos taurus Proteins with correct disulfide bonds ?
ribonuclease + dithiothreitol
-
 Bos taurus ?
-
 ?

Subunits

Subunits Comment Organism
? x * 57000, SDS-PAGE Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Bos taurus

pH Range

pH Minimum pH Maximum Comment Organism
7.2 8 activities are greater than 50% in this range Bos taurus