Changes of haemolymph proteins in Pieris rapae L. during the cuticle formation and hardening process

배추흰나비의 큐티클 形成과 硬化에 따른 혈림프 단백질의 變化

  • Published : 1980.01.01

Abstract

Changes and possible origin of haemolymph proteins during the cuticle formation and hardening are determined by means of acrylamide gel electrophoresis and immunodiffusion. The results by acrylamide gel electrophoresis showed at least 19 protein bands in the haemolymph and 13 fractions in the fat body with relatively constant pattern during the period of cuticle formation and hardening. Both haemolymph and fat body proteins are generally characterized by the presence of three to four heavy stained bands and several thin bands near the top region of the gel. At least over five haemolymph proteins are constantly present during this period. Immunodiffusion tests show that of total eight to nine pupal haemolymph proteins two proteins were already detected in the fat body before pupation and other two proteins were also found in the fat body immediately after pupation, suggesting fat body as possible source of these two haemolymph proteins.

큐티클 形成 및 硬化過程中 血蛋白質의 變化와 起源을 규명하고자 acrylamide gel electrophoresis와 immunodiffusion 方法을 使用하였다. Acrylamide gel electrophoresis에서 적어도 19개의 protein band가 혈림프에서 發見되었으며 脂肪體에서는 13개의 band가 確認되었는데 이들은 대체적으로 일정한 pattern을 유지하였다. 또한 혈림프와 脂肪體의 一般的인 protein band의 pattern은 $3\\sim4$개의 강하게 染色된 band와 몇 개의 가는 band가 gel의 상단에 存在하는 것이 특징이었고 적어도 5개 이상의 haemolymph protein band가  期初에 걸쳐 일정하게 나타났다. Immunodiffusion test에서는 $8\\sim9$개의 血蛋白質에  期初에서 나타났는데 그중 2개의 血蛋白質은  期前에 나타났으며 다른 두 血蛋白質도  化직 후 脂肪體에서 나타남으로써 脂肪體가 이들 血蛋白質의 起源임을 암시하였다.

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