Evidence for the presence of an endogenous inhibitor of prolyl hydroxylase
Document Type
Article
Date of Original Version
1-1-1980
Abstract
Prolyl hydroxylase [EC 1.14.11.2] was shown to be inhibited by an ultrafiltrate (less than 30,000 molecular weight) fraction isolated from skin and blood of neonatal and adult rabbits. This fraction also inhibited two other α-ketoglutarate requiring mixed function oxidases, lysyl hydroxylase [EC 1.14.11.4] and α-butyrobetaine hydroxylase [EC 1.14.11.1] but not the amine oxidase, lysyl oxidase. Purification of the skin ultrafiltrate on Sephadex G-25 demonstrated a peak of prolyl hydroxylase inhibitory activity which chromatographed at a molecular weight corresponding to approximately 3,000. Chromatography of a blood ultrafiltrate separated a similar peak of material which was inhibitory for prolyl hydroxylase.
Publication Title, e.g., Journal
Research Communications in Chemical Pathology and Pharmacology
Volume
29
Issue
2
Citation/Publisher Attribution
Chichester, C. O., and G. C. Fuller. "Evidence for the presence of an endogenous inhibitor of prolyl hydroxylase." Research Communications in Chemical Pathology and Pharmacology 29, 2 (1980): 329-338. https://digitalcommons.uri.edu/bps_facpubs/248
