Open AccessComparison of the NH 2 ‐Terminal Sequences of Chick Type I Preprocollagen Chains Synthesized in an mRNA‐Dependent Reticulocyte Lysate
Author(s) -
GRAVES Peter N.,
OLSEN Bjørn R.,
FIETZEK Peter P.,
PROCKOP Darwin J.,
MONSON Janet M.
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb06411.x
Subject(s) - reticulocyte , messenger rna , lysis , peptide , translation (biology) , proteinase k , biology , peptide sequence , amino acid , microbiology and biotechnology , biochemistry , alpha (finance) , rna , protein biosynthesis , chemistry , gene , enzyme , medicine , construct validity , nursing , patient satisfaction
RNA was extracted from 17‐day‐old chick embryo calvaria and translated by an mRNA‐dependent reticulocyte lysate. Procedures were developed for purifying intact proα1(I) and proα2 translation products from the lysate. These products were identified by comparing tryptic peptide elution patterns of the translation products with those obtained from secreted proα 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 proα chain, and that the two sequences are not the same. Also, the bacterial collagenase‐resistant peptide from the amino terminus of preproα1(I) had an apparent molecular weight which was 10000 greater than the peptide from proα1(I).