Hue H K, Benyamin Y, Roustan C
Centre de Recherches de Biochimie Macromoléculaire, U 249 (INSERM), Université de Montpellier, France.
J Muscle Res Cell Motil. 1989 Apr;10(2):135-42. doi: 10.1007/BF01739969.
The immunological similarities or differences between various actins from muscles of invertebrates were investigated. We elicited antibodies to actin purified from the adductor muscle of the mollusc, Pecten maximus. The antiserum comprised a major population that was specific for the N-terminal extremity of this isoform. This antibody population was used together with other antibodies specific for various domains on the surface of skeletal muscle actin to compare seven actins from invertebrate muscles. The N-terminal extremity showed close homologies between invertebrates (except for Crustacea) but differences were observed with vertebrate skeletal and cytoplasmic actins. In contrast, sequence 18-28, which constitutes part of the myosin interaction domain, appears to be conserved in all actins studied. Other regions (sequences 40-113, 168-226 and 285-375) presented a variable behaviour depending on the particular invertebrate species.
对来自无脊椎动物肌肉的各种肌动蛋白之间的免疫学相似性或差异进行了研究。我们制备了针对从软体动物大扇贝的闭壳肌中纯化的肌动蛋白的抗体。抗血清包含一个主要群体，该群体对这种同工型的N末端特异。该抗体群体与其他针对骨骼肌肌动蛋白表面各种结构域的特异性抗体一起用于比较七种来自无脊椎动物肌肉的肌动蛋白。N末端在无脊椎动物（除甲壳纲动物外）之间显示出密切的同源性，但与脊椎动物的骨骼肌和细胞质肌动蛋白存在差异。相比之下，构成肌球蛋白相互作用结构域一部分的序列18 - 28在所有研究的肌动蛋白中似乎是保守的。其他区域（序列40 - 113、168 - 226和285 - 375）根据特定的无脊椎动物物种表现出可变的行为。
