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KMID : 0378019830260120115
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New Medical Journal
1983 Volume.26 No. 12 p.115 ~ p.120
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Studies of Rabbit Thymocyte NAD Glycohydrolase
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Abstract
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Several properties of the enzyme nicotinamide adenine dinucleotide glycohydrolase (NADase) from rabbit thymocytes, a pH optimum of 6.8, a Km value of 4mM, 50% inhibition by nicotinamide of 6mM, 30% inhibition by INH of 20mM, ability to form NAD analogs, have been measured.
Rabbit thymocyte NADase was compared with the NADase from the other lymphocytes including splenocytes (nylon adherent and nylon nonadherent cells) and bone marrow cells in their specific activities. NADase activity of the thymocytes was lowest among them, suggesting T-lymphocytes have lower NADase activity than B-lymphocytes.
Rabbit thymocytes subcellular organelles were fractionated by sucrose density gradient and measured their NADase activities and plasma membrane fraction has highest specific activity.
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