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Literature summary for 5.3.4.1 extracted from

  • Lambert, N.; Freedman, R.B.
    Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure (1983), Biochem. J., 213, 225-234.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.4.1

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
 2 * 57000, SDS-PAGE under reducing and nonreducing conditions, association between subunits is noncovalent Bos taurus
107000
-
 gel filtration Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein very small carbohydrate content, 0.5-1.0% Bos taurus

Purification (Commentary)

Purification (Comment) Organism
-
 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 incorrectly disulfide-linked ribonuclease Bos taurus Proteins with correct disulfide bonds ?

Subunits

Subunits Comment Organism
dimer 2 * 57000, SDS-PAGE under reducing and nonreducing conditions, association between subunits is noncovalent Bos taurus