Partial characterization of the adenosine deaminase purified from the scallop (Patinopecten yessoensis) midgut gland
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Abstract 1. 1. The purified enzyme (M r = ca 140,000 Da) was a glycoprotein with zinc, and one subunit band (M r = 60,000 Da) was found in SDS-PAGE. 2. 2. The enzyme was stable in the acid pH range, active at pH 6.0 and irreversibly denatured by urea and guanidine. 3. 3. The K m and k cal values for adenosine were 30 μM and 170/sec, respectively. V max / K m varied, but V max did not, with pH changes between 5.5 and 7.0. The apparent activation energies for V max / K m and V max were 0 and 12 kcal/mol in the temperature range below 37°C, respectively. 4. 4. Inosine was competitive inhibitor ( K i = 510 μ M). Inhibition by p -chloromercuribenzoate was time-dependent and the two binding sites were suggested.
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 105 51-61, 1993-05-01
Elsevier BV