A Monoclonal Antibody Specific for the Amino Terminal Cleavage Site of Procollagen Type I

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Abstract
A monoclonal mouse IgG1 antibody was produced against the aminopropetide of dermatosparactic sheep procollagen type I by using the hybridoma technique. Radioimmunoassays demonstrated an apparent affinity constant of 1081 · 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 aminopropetide 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.