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Studies of human pituitary LH containing internally cleaved beta subunit
A Stockell Hartree1, R C Shownkeen
1AFCR Institute of Animal Physiology and Genetics Research, Babraham, Cambridge.
Journal of Molecular Endocrinology
|February 1, 1991
Summary
Internal peptide bond cleavage in human luteinizing hormone (hLH) beta subunits was investigated. This nicking affects subunit interaction and receptor binding, with methods developed to produce nick-free hLH.
Area of Science:
- Biochemistry
- Endocrinology
- Protein Chemistry
Background:
- Pituitary human luteinizing hormone (hLH) exhibits internal peptide bond cleavage in its beta subunit.
- The prevalence of this cleavage varies between preparation batches.
Purpose of the Study:
- To investigate the origin and effects of beta subunit cleavage in hLH.
- To develop methods for producing nick-free hLH.
Main Methods:
- Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) to assess cleaved beta subunit.
- Urea dissociation, dialysis, and reassociation of subunits.
- Inhibition using phenylmethylsulphonyl fluoride (PMSF) and EDTA.
- Purification using Sephadex G-100 gel filtration.
Main Results:
- Cleavage of the beta subunit was observed in hLH and, to a lesser extent, in hTSH, but not in hFSH or hCG.
- Urea dissociation followed by dialysis increased beta subunit nicking, preventable by PMSF and EDTA.
- A method was established to obtain virtually nick-free hLH.
Conclusions:
- The study elucidates the origin of beta subunit cleavage in hLH.
- Protease inhibitors and chelating agents can prevent this cleavage.
- A protocol for producing purified, nick-free hLH was successfully developed.
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