Department of Botany, The University of Texas at Austin, Austin, Texas 78712.
Plant Physiol. 1984 Jun;75(2):382-6. doi: 10.1104/pp.75.2.382.
A protein identifiable as calmodulin has been isolated from oat (Avena sativa, var Garry) tissues. This protein is relatively heat stable, binds to hydrophobic gels, and phenothiazines in a calcium-dependent fashion, and binds to antibody to rat testes calmodulin. Based on its migration on sodium dodecyl sulfate-polyacrylamide gels, ultraviolet absorption spectrum, and amino acid composition, oat calmodulin is essentially identical to calmodulin isolated from other higher plants. Radioimmunoassays indicate that calmodulin is associated with isolated oat protoplasts, mitochondria, etioplasts, and nuclei and also appears to be a component of oat cell wall fractions.
已从燕麦(Avena sativa,var Garry)组织中分离出一种可识别的钙调蛋白。该蛋白耐热性相对较强,能以钙离子依赖的方式与疏水凝胶和吩噻嗪结合,并与抗大鼠睾丸钙调蛋白的抗体结合。根据其在十二烷基硫酸钠-聚丙烯酰胺凝胶上的迁移、紫外吸收光谱和氨基酸组成,燕麦钙调蛋白与其他高等植物分离的钙调蛋白基本相同。放射免疫测定表明,钙调蛋白与分离的燕麦原生质体、线粒体、前质体和核结合,也似乎是燕麦细胞壁部分的组成部分。