1997 年 63 巻 5 号 p. 784-793
Histological and biochemical changes of collagen in the kuruma prawn Penaeus japonicus muscle during chilled storage were examined. In histological experiments, a partial disintegration of thin connective tissues, endomysium and perimysium, where a specific α component, α2 (AR-I), mainly distributed, was observed in the prawn muscle stored for 24h at 5°C, while the structure of the thick connective tissue, epimysium, did not so changed. On the other hand, a preferentialdecrease in the relative staining intensity of the components reactive for the anti-α2 (AR-I) component serum was detected by immunoblot analysis of guanidine hydrochloride-soluble collagen from the muscle stored for 24h at 5°C, while the α1 (AR-I) component or Type AR-II collagen did not so affected. These combined results suggest that the disintegration of the thin connective tissues is due to some biochemical changes of α2 (AR-I)-related components.