Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A.

Protein disulfide isomerase (PDI, EC 5.3.4.

Human spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein with oxidizing activity.

Spermatid-specific thioredoxin-1 (Sptrx-1) is the first member of the thioredoxin family of proteins with a tissue-specific expression pattern, found exclusively in the tail of elongating spermatids and spermatozoa. We describe here further biochemical characterization of human Sptrx-1 protein structure and enzymatic activity. In gel filtration chromatography human Sptrx-1 eluates as a 400 kDa protein consistent with either an oligomeric form, not maintained by intermolecular disulfide bonding, and/or a highly asymmetrical structure.