title: Detection of collagen degradation products from subcutaneously implanted organic bone matrix.
abstract: Demineralized bovine bone powder was reduced with NaB3H4 to label the collagen crosslinks with tritium. The powder was enclosed in small nylon mesh pouches and implanted subcutaneously into rats for 3 weeks. Histological examinations revealed that multinuclear giant cells accumulated around the bone matrix, some in Howship's lacunae. Collagenous peptides containing intermolecular crosslinks were detected in the urea-soluble fraction extracted from the implant. Two crosslink-containing peptides were isolated from a dialyzable fraction: one contained dihydroxylysinonorleucine and the other hydroxylysinonorleucine. Both peptides had molecular weights of approximately 1000 estimated from the elution positions of gel filtration chromatography; and both had similar quantitative compositions of amino acids. There were no homologous peptides detected in a control experiment of the reduced bone matrix which was incubated in vitro with buffered saline for 1 week at 37 degrees C.
mesh_terms: D000818:Animals; D001857:Bone Matrix / Q000032:analysis / Q000033:anatomy & histology / Q000637:transplantation*; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000032:analysis* / Q000378:metabolism; D062109:Dermatologic Surgical Procedures; D051381:Rats; D014183:Transplantation, Heterologous; D014316:Tritium
chemical_list: D014316:Tritium; D003094:Collagen