Purification and properties of gut arginase from earthworm Pheretima communissima
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説明
Abstract 1. 1. Arginase from Pheretima communissima was purified about 10,000-fold and its properties were compared with those of the same enzyme in other organisms. 2. 2. The molecular weight of the enzyme, as determined by gel filtration on Sephadex G-100, was about 25,000, which is substantially less than that of the subunits of oligomeric arginases. 3. 3. The arginase was extremely labile, losing 90% of its original activity by dialysis against a Mn2+-free buffer for 4 hr. Seventy percent of its original activity was recovered following treatment with 1 mM MnCl2 at 37°C for 20 min. 4. 4. The K m values for l -arginine were 8.5 mM at pH 9.5 and 54 mM at pH 7.5, respectively and the activity was competitively inhibited by l -ornithine and l -lysine, and caused a mixed-type inhibition by l -leucine, l -isoleucine and l -valine at both pHs.
収録刊行物
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- Comparative Biochemistry and Physiology Part B: Comparative Biochemistry
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Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 83 79-84, 1986-01-01
Elsevier BV
