Open AccessProcollagen Processing
Author(s) -
DAVIDSON Jeffrey M.,
MCENEANY Linda S. G.,
BORNSTEIN Paul
Publication year - 1979
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1979.tb04201.x
Subject(s) - pepstatin , leupeptin , protease , proteolysis , procollagen peptidase , biochemistry , cathepsin , chemistry , gel electrophoresis , sodium dodecyl sulfate , concanavalin a , size exclusion chromatography , enzyme , microbiology and biotechnology , biology , in vitro
An enzymatic activity, capable of removing the COOH‐terminal extensions of type I chick procollagen, has been demonstrated in embryonic chick tendons and in cultured tendon fibroblasts utilizing two new methods of analysis. The protease was purified by a combination of ultrafiltration, concanavalin A affinity chromatography and gel filtration. The isolated protein has an apparent M r of 43000 by gel filtration and sodium dodecyl sulfate gel electrophoresis. The enzyme shows a major pH optimum at 4.2 and is susceptible to inhibitors such as pepstatin and leupeptin; it therefore seems related to the cathepsins. The possibility that this enzyme plays a role in the limited proteolytic processing of procollagen is discussed.