Comparison of the NH2‐Terminal Sequences of Chick Type I Preprocollagen Chains Synthesized in an mRNA‐Dependent Reticulocyte Lysate

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Abstract
RNA was extracted from 17 day old chick embryo calvaria and translated by an mRNA-dependent reticulocyte lysate. Procedures were developed for purifying intact pro.alpha.1[procollagen](I) and pro.alpha.2 translation products from the lysate. These products were identified by comparing tryptic peptide elution patterns of the translation products with those obtained from secreted pro.alpha. chains. Partial sequence data from the amino terminus of each translation product demonstrated that each chain begins with a sequence that is different from that of the corresponding pro.alpha. chain, and that the 2 sequences are not the same. Also, the bacterial collagenase-resistant peptide from the amino terminus of prepro.alpha.1(I) had an apparent MW which was 10,000 greater than the peptide from pro.alpha.1(I).