Localization and isozyme patterns of phosphatase in Fibricola seoulensis

Fibricola seoulensis에서 phosphatase의 분포와 동위효소유형

The present study was carried out to investigate the localization and isozyme patterns of acid phosphatase and alkaline phosphatase in metacercariae and in adults of F. seoulensis by enzyme-histochemistry method and electrophoresis. Acidphosphatase showed a strong activity at pH 5 in the intestinal caecum of adults, but showed no reactions in the nonsubstrate control and in the inhibitor-treated control. Alkaline phosphatase showed a strong activity at pH 8 in the intestinal caecum and the tribocytic organ of adults, and in the intestinal caecum and in the genital anlagen of metacercariae. In non-denature PAGE, ten bands of protein fraction from the extracts of metacercariae and twenty-two bands from adults were detected. In denature PAGE, two protein bands having molecular weights of 192 kDa and 123 kDa were detected in the metacercariae, but absent from adult stage. In adults, protein fractions of 27.5 kDa, 24.5 kDa, 21.4 kDa, 18 kDa, 16 kDa and 15 kDa were detected. In non-denature PAGE, isozymes of acid phosphatase showed the most strong activity at pH 5, whereas no activity was shown at pH 2 and pH 7. One isozyme 85 kDa, 73 kDa and 62 kDa) in adults.

Fibricola seoulensis의 성체와 피낭유충에서 acid(Acpase)와 alkaline phosphatase (AIPase)의 분포와 동위효소유형 (유형)의 변화를 추구하고자 효소조직화학적 방법과 전기영동법을 이용하여 성체에서 Acpase는 pH 5가 최적의 활성이 나타났고. 분자량이 95 kDa. 85 kDa. 73 kDa. 62 kDa인 4종류의 동위효소가 동정되었다. 피낭유충에서 A쳬ase는 활성이 약하거나 나타나지 않았고. 분자량이 62 kDa인 1종류의 동위효소가 동정되었다 성체와 피낭유충에 AIPase는 pH 8에서 최적의 활성이 나타났고, 피낭유충의 생식원기에서 강한 활성이 나타났다.