Crossref
journal-article
Wiley
FEBS Letters (311)
Abstract
The decapeptide gonadotropin‐releasing hormone (GnRH) is degraded by the 20 S multicatalytic proteinase complex (proteasome EC 3.4.99.46), purified from ovarian granulosa cells, at the Tyr5 Gly6 bond and to a lesser extent at the Gly6 Leu7 bond, when incubated for 2 h at 37°C. Further cleavage, at Trp3 Ser4 and Ser4 Tyr5 bonds of the neurohormone occurs only subsequently to the appearance of the initial N‐terminal degradation products, (1–5)GnRH and (1–6)GnRH. Our results suggest that the sequential degradation of GnRH can serve as an important mechanism for the rapid termination of its biological activity in target cells.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 25, 2002, 3:40 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 8:56 a.m.) |
Indexed | 1 year, 1 month ago (July 12, 2024, 8:34 a.m.) |
Issued | 31 years, 2 months ago (June 13, 1994) |
Published | 31 years, 2 months ago (June 13, 1994) |
Published Online | 23 years, 7 months ago (Jan. 9, 2002) |
Published Print | 31 years, 2 months ago (June 13, 1994) |