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XB-ART-56756
Eur J Biochem 1983 Jul 15;1341:183-9. doi: 10.1111/j.1432-1033.1983.tb07549.x.
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A monoclonal antibody specific for the amino terminal cleavage site of procollagen type I.

Foellmer HG , Kawahara K , Madri JA , Furthmayr H , Timpl R , Tuderman L .


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A monoclonal mouse IgG1 antibody was produced against the aminopropeptide of dermatosparactic sheep procollagen type I by using the hybridoma technique. Radioimmunoassays demonstrated an apparent affinity constant of 10(8) l X mol-1. The antibody reacted with a 19-amino-acid-long sequence spanning the procollagen N-proteinase cleavage site with stronger binding to structures contributed by the aminopropeptide. The antibody showed strong cross-reactions with similar antigens of bovine, human or chick origin but failed to react with the aminopropeptide of procollagen type III. Incubation of chick or sheep procollagen type I with stoichiometric amounts of antibody blocked the release from procollagen molecules of the aminopropeptide by procollagen N-proteinase. Thus, this antibody seems useful for studying various biological problems encountered in the conversion of procollagen.

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