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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Costell M,Grisolía Sdoi
10.1016/0006-291x(85)91698-5subject
Has Abstractpub_date
1985-04-16 00:00:00pages
441-8issue
1eissn
0006-291Xissn
1090-2104pii
0006-291X(85)91698-5journal_volume
128pub_type
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