Histochemical studies on the olfactory epithelium of some hillstream teleosts

Living specimens of Barilius bendelisis, Crossocheilus latius latius, Torputitora, Glyptothorax pectinopterus and Pseudecheneis sulcatus were collected from the streams and rivers of Garhwal Himalaya. Histochemical localization of carbohydrates (1:2 glycol groups, glycogen, B-metachromasia and acid mucopolysaccharides), proteins and protein bound NH sub(2) group, bound lipids and the enzymes (acid and alkaline phosphatases) in the olfactory epithelium were studied. The receptor, supporting basal and mucous cells show varying degrees of distinction and distribution of these substances. The enzymes are present on the surface of the epithelium, sensory hairs and the boundaries of mucous cells only.

Role of transglutaminase-mediated cross-linking of protein in the temperature-dependent setting of Alaska pollack surimi

During the low temperature setting of fish paste, myosin heavy chain (MHC) is polymerized to cross-linked myosin heavy chain (CMHC), which is considered to occur by the action of endogenous transglutaminase (TGase). In this study the contribution of TGase on the setting of Alaska pollack surimi at different temperatures was studied. Alaska pollack surimi was ground with 3% NaCl, 30% h2o and with or without ethylene glycol bis (β-aminoethylether) N, N, N¹,N¹- tetra acetic acid (EGTA), an inhibitor of TGase. Among the pastes without EGTA, highest TGase activity was observed at 25°C but breaking force of the gel set at 25°C was lower than that set at 30°, 35°, and 40°C. Addition of EGTA (5m mol/kg) to the paste suppressed TGase activity at all setting temperatures from 20° to 40°C. Gelation of the pastes and cross-linking of MHC on addition of EGTA were suppressed completely at 20° and 25°C, partially at 30° and 35°C, and not at all at 40°C. The findings suggested that during the setting of Alaska pollack surimi TGase mediated cross-linking of MHC was strong at around 25°C but the thermal aggregation of MHC by non-covalent bonds was strong at above 35°C. Setting of surimi at 40°C and cross-linking of its MHC did not involve TGase.