HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Knox, W. E. Articles by Piras, M. M. Search for Related Content PubMed PubMed Citation Articles by Knox, W. E. Articles by Piras, M. M. Social Bookmarking                      What's this?

A Reinterpretation of the Stabilization of Tryptophan Pyrrolase by Its Substrate

From the ¹ From the Department of Biological Chemistry, Harvard Medical School, and the Cancer Research Institute, New England Deaconess Hospital, Boston, Massachusetts 02215

The loss of activity of the liver tryptophan pyrrolase when it is incubated without tryptophan can be reversed. Crude tryptophan pyrrolase preparations, in general, are slowly activated by incubation with tryptophan, methemoglobin, and ascorbate, during which conjugation of the apoenzyme and its reduction to the active, reduced holoenzyme occurs. Aerobic incubation without tryptophan inactivates without unconjugating the enzyme, apparently by forming the reversibly inactivated, oxidized holoenzyme. It can be reactivated by prior incubation with tryptophan and ascorbate.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?