Biochemical Characterization of Collagen in Myocommata and Endomysium Fractions of Carp and Spotted Mackerel Muscle

Abstract

Preparation of myocommata and endomysium fractions Myocommata and endomysium fractions were prepared from the different parts of body muscle of carp and spotted mackerel. Both type I and V collagens were detected in the myocommata and endomysium fractions of both fish. The relative concentration of type V collagen to type I collagen was higher in the endomysium fraction than in the myocommata fraction. Both type I and V collagens were less soluble in the endomysium fraction than in the myocommata fraction. These results indicated that the biochemical property of the collagen in the pericellular connective tissue was different from that of the collagen in the interstitial connective tissue of fish.

Changes in muscle collagen content during post mortem storage of farmed sea bream (Sparus aurata): influence on textural properties

“…This is a colorimetric method based on the oxidation of hydroxyproline with chloramine-T, followed by the addition of 4-dimethylaminobenzaldehyde, producing a coloured complex that was measured spectro-photometrically at 560 nm. To convert the quantity of hydroxyproline into collagen, a factor of 11.42 was used (Sato et al 1989) and expressed as mg/g fresh weight.…”

Characterization and Comparison of Collagens Extracted From the Digestive Tract and Skin of a Japanese Amberjack Seriola Quinqueradiata

“…1988). An aliquot of ASC was digested with pepsin to detect the presence of type V collagen by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE), as described previously (Sato et al. 1989b).…”

“…The amounts of the types I and V collagens in the ASC, PSC and ISC preparations were calculated on the basis of the hydroxyproline content of the hydrolyzates and the relative staining intensity of type V collagen α1(V) band as compared with the total collagenous bands on SDS‐PAGE gels, as described previously (Sato et al. 1989b).…”

Post-mortem changes of muscle from fresh water prawn (Macrobrachium rosenbergii) as influenced by spawning stages

“…2). Sato, Yoshinaka, Sato, and Tomita (1989) reported that the major collagen from the crustacean muscle was similar to type V collagen from the vertebrate muscle. The solubility of rainbow trout type V collagen increased during storage in ice, while no change in type I was observed, which may suggest that type V collagen is involved in the rapid softening of fish muscle (Sato, Ohashi, Ohtsuki, & Kawabata, 1991).…”