The isolation of glycoproteins from bovine achilles tendon and their interaction with collagen.
Two glycoprotein fractions, A and B, were isolated from bovine achilles tendon. Glycoprotein A was prepared from a 0.2m-sodium chloride extract and glycoprotein B was isolated from a 3m-magnesium chloride extract. They were free from serum proteins. Glycoprotein A was essentially free of collagen, but glycoprotein B contained about 8% collagen. Both glycoproteins gave several bands on isoelectric focusing. This technique was also used to demonstrate that both glycoprotein fractions interacted strongly with acid-soluble calf skin tropocollagen. It is concluded that these fractions are true components of tendon, and that they may have some function in the macromolecular organization of the tissue.
D000125:Achilles Tendon / Q000032:analysis*; D000818:Animals; D002417:Cattle; D002712:Chlorides; D003094:Collagen; D006023:Glycoproteins / Q000302:isolation & purification*; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D046911:Macromolecular Substances; D008274:Magnesium; D012867:Skin; D012965:Sodium Chloride; D014461:Ultracentrifugation
D002712:Chlorides; D006023:Glycoproteins; D046911:Macromolecular Substances; D012965:Sodium Chloride; D003094:Collagen; D008274:Magnesium