Neutral metallo-proteinases of rabbit bone. Separation in latent forms of distinct enzymes that when activated degrade collagen, gelatin and proteoglycans.
Rabbit bones in culture produce specific collagenase and neutral metallo-proteinase activity in latent forms that can be activated by either 4-aminophenylmercuric acetate or trypsin. Latent neutral metallo-proteinase activity was resolved by gel filtration into two enzymes, distinct from collagenase, that degrade gelatin and cartilage proteoglycans.
D000818:Animals; D001842:Bone and Bones / Q000201:enzymology*; D003094:Collagen / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation; D005780:Gelatin / Q000378:metabolism; D008667:Metalloproteins / Q000378:metabolism*; D003012:Microbial Collagenase / Q000378:metabolism; D009924:Organ Culture Techniques; D011509:Proteoglycans / Q000378:metabolism; D011817:Rabbits
D008667:Metalloproteins; D011509:Proteoglycans; D005780:Gelatin; D003094:Collagen; D010450:Endopeptidases; D003012:Microbial Collagenase