Post-mortem changes of types I and V collagens in rainbow trout muscle were examined in relation to the softening of fish muscle during chilled storage. Degradation of helical regions of collagens was not detected. On the other hand, the solubility of type V collagen increased significantly, while that of type I collagen did not change. These facts suggest that degradation of nonhelical regions or intermolecular cross-links occur preferentially in type V collagen.
机构:
TOKYO MED & DENT UNIV, MED RES INST, DEPT TISSUE PHYSIOL, CHIYODA KU, TOKYO 101, JAPANTOKYO MED & DENT UNIV, MED RES INST, DEPT TISSUE PHYSIOL, CHIYODA KU, TOKYO 101, JAPAN
ADACHI, E
HAYASHI, T
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TOKYO MED & DENT UNIV, MED RES INST, DEPT TISSUE PHYSIOL, CHIYODA KU, TOKYO 101, JAPANTOKYO MED & DENT UNIV, MED RES INST, DEPT TISSUE PHYSIOL, CHIYODA KU, TOKYO 101, JAPAN
机构:
TOKYO MED & DENT UNIV, MED RES INST, DEPT TISSUE PHYSIOL, CHIYODA KU, TOKYO 101, JAPANTOKYO MED & DENT UNIV, MED RES INST, DEPT TISSUE PHYSIOL, CHIYODA KU, TOKYO 101, JAPAN
ADACHI, E
HAYASHI, T
论文数: 0引用数: 0
h-index: 0
机构:
TOKYO MED & DENT UNIV, MED RES INST, DEPT TISSUE PHYSIOL, CHIYODA KU, TOKYO 101, JAPANTOKYO MED & DENT UNIV, MED RES INST, DEPT TISSUE PHYSIOL, CHIYODA KU, TOKYO 101, JAPAN