Chemical and structural differences between cilia and flagella from the lamellibranch mollusc, Aequipecten irradians

作者：Richard W. Linck · 发表于：Journal of Cell Science · 年份：1973 · DOI：10.1242/jcs.12.3.951 · 被引用次数：105 · 研究领域：Hemoglobin structure and function、Mass Spectrometry Techniques and Applications、Microtubule and mitosis dynamics

ABSTRACT Gill cilia and sperm flagella from the lamellibranch mollusc Aequipecten irradians were isolated by several methods and chemically fractionated by low-ionic-strength dialysis. These organelles differ in their forms of dynein and in the stabilities of their homologous microtubules and subsidiary structures (i.e. nexin fibres and spoke material). In flagella more than 80% of the axoneme ATPase is solubilized, appearing as a 14s peak in the ultracentrifuge, and the whole axoneme is broken down to unlinked, doublet outer fibres. In cilia only half of the ATPase is solubilized from axonemes as a 14S component. The ciliary B-tubules and one member of the central pair also dissolve, leaving the A-tubules and the other central tubule held together by nexin fibres and matrix material as a 9 + 1 singlet axoneme, to which is bound the remaining half of the ATPase. This tightly bound form of the ciliary ATPase can be removed in an enzymically active form by brief trypsin treatment which causes the breakdown of the singlet axoneme. The trypsin-solubilized ATPase behaves like native 14s dynein in the ultracentrifuge but breaks down to polypeptides when electrophoresed in the presence of sodium dodecyl sulphate (SDS). The native 14 s material containing the dynein was partially purified by column chromatography and was shown on SDS-polyacrylamide gels to be composed of 2 components. The molecular weights of these as determined by 3% acrylamide SDS-gels are 450000 and 500000, and th...