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Science 15 June 1973:
Vol. 180. no. 4091, pp. 1188 - 1190
DOI: 10.1126/science.180.4091.1188
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Articles

Synthesis of the Pyrrole Porphobilinogen by Sepharose-Linked dgr-Aminolevulinic Acid Dehydratase

Daniela Gurne 1 and David Shemin 1

1 Biochemistry Division, Department of Chemistry, Northwestern University, Evanston, Illinois 60201

dgr-Aminolevulinic acid dehydratase from Rhodopseudomonas spheroides was covalently linked to Sepharose 4B, which had been activated with cyanogen bromide. A column containing this enzyme gel readily catalyzed the synthesis of the pyrrole porphobilinogen on continuous passage of a solution of dgr-aminolevulinic acid. Under the conditions of the procedures, product inhibition was minimized and a 50 to 94 percent yield was attained. A column containing about 1 milligram of enzyme was continuously operated for 27 days. Although its total activity appeared to be reduced about 30 percent at the end of this time, the bound enzyme produced approximately 200 milligrams of porphobilinogen each day, and about 5 grams of the pyrrole were isolated.

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Science. ISSN 0036-8075 (print), 1095-9203 (online)