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High post-translational modification levels in type II procollagen are not a consequence of slow triple-helix
Abstract:
The kinetics of triple helix formation of newly synthesized type II procollagen in chick embryo sternal cartilage cells were determined. The data obtained were in agreement with a model for triple helix formation in cellulo proposed recently (Bruckner et al., 1981). The time required to produce fully triple helical type II procollagen in cartilage cells was only 30% longer than for type I procollagen in tendon cells. Therefore, the several-fold increase in post-translational modification observed for type II collagen as compared to type I collagen cannot be attributed solely to slow helix formation but rather is a result of higher levels of enzymic activity of post-translational modification present in cartilage cells.