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January 5, 1990Science

Evidence for a Novel Thioredoxin-Like Catalytic Property of Gonadotropic Hormones

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Authors

JBJ. Jay BonifaceVPDiagnostics (United States)LRLEO E. REICHERTBavarian State Research Center for Agriculture

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Implication

Biochemical analysis reveals potent thioredoxin-like catalytic activity in purified gonadotropic hormones, indicating a novel enzymatic mechanism in hormone-receptor activation.

Key Points

  • Determine whether gonadotropic hormones contain thioredoxin-like sequence motifs and exhibit disulfide isomerase catalytic activity.
  • Examined amino acid sequences of gonadotropic hormone beta subunits for homology with the active site of thioredoxin.
  • Assayed catalytic disulfide isomerase activity of purified ovine follicle-stimulating hormone and bovine luteinizing hormone by measuring the reactivation of reduced, denatured ribonuclease.
  • Sequence analysis identified a conserved thioredoxin active-site tetrapeptide (Cys-Gly-Pro-Cys) in the beta subunit of luteinizing hormone and a related sequence (Cys-Gly-Lys-Cys) in follicle-stimulating hormone.
  • Purified ovine follicle-stimulating hormone and bovine luteinizing hormone were approximately 60 times and approximately 300 times more active than thioredoxin on a molar basis, respectively.

Cite This Study

Boniface et al. (1990) studied this question.

synapsesocial.com/papers/6a82d4025bcab2ccdb8d7005https://doi.org/10.1126/science.2104678
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