In:
FEBS Letters, Wiley, Vol. 321, No. 2-3 ( 1993-04-26), p. 205-208
Abstract:
Prostaglandin H synthase (PGHS) as apo‐PGHS, holo‐PGHS, and holo‐PGHS, inactivated in the course of catalysis was studied using chemical modification with diethyl pyrocarbonate (DEPC). The exhausted reaction with DEPC corresponded to the modification of 7 histidine residues in apo‐PGHS and 4 in holo‐PGHS. All 18 histidine residues became accessible for modification with DEPC in the enzyme, inactivated in the course of catalysis. The velocities of tryptic cleavage of all the three forms into two fragments were fairly different but independent of modification. Based on the results we hypothesize fast and dramatic changes in the protein structure in the course of the substrate conversion.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(93)80109-8
Language:
English
Publisher:
Wiley
Publication Date:
1993
detail.hit.zdb_id:
1460391-3
SSG:
12
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