Department of Biology, Queen's University, Kingston, Ontario K7L 3N6 Canada.
Plant Physiol. 1981 Oct;68(4):827-30. doi: 10.1104/pp.68.4.827.
All the glutamate dehydrogenase activity in developing castor bean endosperm is shown to be located in the mitochondria. The enzyme can not be detected in the plastids, and this is probably not due to the inactivation of an unstable enzyme, since a stable enzyme can be isolated from castor bean leaf chloroplasts. The endosperm mitochondrial glutamate dehydrogenase consists of a series of differently charged forms which stain on polyacrylamide gel electrophoresis with both NAD(+) and NADP(+). The chloroplast and root enzymes differ from the endosperm enzyme on polyacrylamide gel electrophoresis. The amination reaction of all the enzymes is affected by high salt concentrations. For the endosperm enzyme, the ratio of activity with NADH to that with NADPH is 6.3 at 250 millimolar NH(4)Cl and 1.5 at 12.5 millimolar NH(4)Cl. K(m) values for NH(4) (+) and NAD(P)H are reduced at low salt concentrations. The low K(m) values for the nucleotides may favor a role for glutamate dehydrogenase in ammonia assimilation in some situations.
发育中的蓖麻胚乳中的所有谷氨酸脱氢酶活性都被证明位于线粒体中。该酶不能在质体中检测到,这可能不是由于不稳定酶的失活,因为可以从蓖麻叶叶绿体中分离出稳定的酶。胚乳线粒体谷氨酸脱氢酶由一系列带不同电荷的形式组成,这些形式在聚丙烯酰胺凝胶电泳中用 NAD(+)和 NADP(+)染色。叶绿体和根中的酶在聚丙烯酰胺凝胶电泳中与胚乳酶不同。所有酶的氨基化反应都受到高盐浓度的影响。对于胚乳酶,在 250 毫摩尔氯化铵和 12.5 毫摩尔氯化铵下,NADH 的活性与 NADPH 的活性之比为 6.3,在 1.5 毫摩尔氯化铵下为 6.3。NH(4)(+)和 NAD(P)H 的 K(m)值在低盐浓度下降低。核苷酸的低 K(m)值可能有利于谷氨酸脱氢酶在某些情况下参与氨同化。