Decarbamoylating activity of ornithine transcarbamoylase.

Abstract:

:We have purified from beef liver an enzyme which decarbamoylates carbamoyl-hemoglobin and to a much lesser extent carbamoyl histones. Carbamoyl casein was a poor substrate while carbamoyl trypsin, fibrinogen and ovoalbumin were not affected. The optimal pH is 7.4. Addition of Mg++, Mn++ or Ca++ was without effect. On testing citrulline as a substrate we found high activity leading us to suspect that the activity of the decarbamoylase preparation was due to contaminating ornithine transcarbamoylase activity. Evidence for this is the similar ratio of transcarbamoylase to decarbamoylase activities of both ornithine transcarbamoylase and of the purified preparation of decarbamoylase from beef liver. Also, delta-PALO, the specific inhibitor of ornithine transcarbamoylase inhibited both preparations to the same extent. Interestingly, ornithine transcarbamoylase from bacteria also has decarbamoylase activity while aspartic transcarbamoylase does not.

authors

Costell M,Grisolía S

doi

10.1016/0006-291x(85)91698-5

subject

Has Abstract

pub_date

1985-04-16 00:00:00

pages

441-8

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(85)91698-5

journal_volume

128

pub_type

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