Identification of two new collagen alpha-chains in extracts of lathyritic chick embryo tendons |
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Authors: | S A Jimenez R Yankowski R I Bashey |
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Affiliation: | Department of Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19174 U.S.A. |
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Abstract: | Two new collagen polypeptide chains have been identified in extracts of lathyritic embryonic chick tendons. The electrophoretic migration of these polypeptides in sodium dodecyl sulfate-polyacrylamide gels indicates that they have about 20% greater apparent molecular weights than α1 and α2 chains of Type I collagen. These chains are not held by disulfide bonds since reduction does not affect their electrophoretic behavior. Further, they do not represent incompletely cleaved procollagen since their apparent molecular size remains greater than that of Type I collagen polypeptides after limited proteolytic digestion. Because the ratio of these polypeptides in the purified extracts is not 2:1 it appears that they are components of two separate tropocollagen molecules. |
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Keywords: | To whom correspondence should be addressed. |
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