Title

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

Research Communications in Chemical Pathology and Pharmacology

Volume

29

Issue

2

Share

COinS