Interaction of collagen molecules from the aspect of fibril formation: acid-soluble, alkali-treated, and MMP1-digested fragments of type I collagen.

@article{Suzuki1999InteractionOC,
  title={Interaction of collagen molecules from the aspect of fibril formation: acid-soluble, alkali-treated, and MMP1-digested fragments of type I collagen.},
  author={Yasuhiro Suzuki and Iori Someki and Eijiro Adachi and Shinkichi Irie and Shunji Hattori},
  journal={Journal of biochemistry},
  year={1999},
  volume={126 1},
  pages={54-67}
}
Collagen type I extracted with acid or digested with pepsin forms fibrils under physiological conditions, but this ability is lost when the collagen is treated with alkaline solution or digested with matrix metalloproteinase 1 (MMP1). When acid-soluble collagen was incubated with alkali-treated collagen, the fibril formation of acid-soluble collagen was inhibited. At 37 degrees C, at which alkali-treated collagen is denatured, the lag time was prolonged but the growth rate of fibrils was not… CONTINUE READING

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