Josefina Caravaca, Ph.D.; E. Grey Dimond, M.D., F.A.C.P.
This content is PDF only. Please click on the PDF icon to access.
A molecular subunit of beef hepatocatalase that exhibits high enzymatic activity as a peroxidase-oxidase and is essentially free of catalatic action has been isolated. The hepatocatalase peroxidase subunit (HCP) is a depolymerization product of hepatocatalase with an estimated molecular weight of 80,000 ± 12,000. It was obtained in the form of a stable, lyophilized, water-soluble powder by a procedure involving alkaline hydrolysis, dialysis, and lyophilization. Like hepatocatalase, HCP is also a porphyrin enzyme. The availability of this preparation has made it possible to study the peroxidatic function of catalase without interference from its catalatic action and to obtain some basic
Learn more about subscription options.
Register Now for a free account.
Caravaca J, Dimond EG. Prevention and Regression of Atherosclerosis by Peroxidase.. Ann Intern Med. 1967;66:1035. doi: 10.7326/0003-4819-66-5-1035_2
Download citation file:
Published: Ann Intern Med. 1967;66(5):1035.
Results provided by:
Copyright © 2017 American College of Physicians. All Rights Reserved.
Print ISSN: 0003-4819 | Online ISSN: 1539-3704
Conditions of Use
This PDF is available to Subscribers Only