Abstract
The purpose of this study was to investigate the chemotactic activity of the bovine dental pulp collagen and collagen peptide fragments using human blood monocytes. Chemotactic assays were performed with the modified Boyden's method. The results obtained were as follows: 1) Non-collagenous proteins and neutral salt-soluble collagen from the bovine dental pulps did not show a high chemotactic activity. 2) Neutral salt-soluble collagen from the skin of fetal bovine had a greater chemotactic activity than that from the dental pulp. 3) Peptide fragments obtained by digesting the above three proteins with CNBr showed a greater chemotactic activity than those proteins themselves. 4) Peptide fragments obtained by digesting theinsoluble proteins, most of which consisted of insoluble collagen, with CNBr had a great chemotactic activity on the human monocytes. The molecular weight of these peptide fragments was thought to be less than 14, 000. 5) Solubilized proteins obtained by digesting insoluble proteins with trypsin and demineralizing them with EDTA showed a greater chemotactic activity on the human monocytes than the peptide fragments derived from the insoluble collagen digested with trypsin.
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