Evidence for the presence of an endogenous inhibitor of prolyl hydroxylase
Date of Original Version
Prolyl hydroxylase [EC 184.108.40.206] 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 220.127.116.11] and α-butyrobetaine hydroxylase [EC 18.104.22.168] 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
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