The M sub(r)-24,000 phosphoprotein from developing bone is the NH sub(2)-terminal propeptide of the alpha 1 chain of type I collagen

Using nondegradative isolation procedures, the authors have purified and characterized the M sub(r) 24,000 phosphoprotein from developing bovine and human bone where it constitutes 5% of the noncollagenous protein in the mineral compartment. The purified, intact product spontaneously formed a comple...

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Bibliographic Details
Published in:The Journal of biological chemistry 1987-01, Vol.262 (28), p.13457-13463
Main Authors: Fisher, L W, Robey, P G, Tuross, N, Otsuka, AL, Tepen, DA, Esch, F S, Shimasaki, S, Termine, J D
Format: Article
Language:English
Subjects:
bone
cattle
man
phosphoproteins
Online Access:Get full text
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Summary:Using nondegradative isolation procedures, the authors have purified and characterized the M sub(r) 24,000 phosphoprotein from developing bovine and human bone where it constitutes 5% of the noncollagenous protein in the mineral compartment. The purified, intact product spontaneously formed a complex consistent with a collagen-like trimer that remained a trimer even in sodium dodecyl sulfate polyacrylamide gels.
ISSN:0021-9258