Comparison of the NH2-Terminal sequences of chick Type I preprocollagen chains synthesized in an nRNA-dependent reticulocyte lysate. Academic Article

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(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 two sequences are not the same. Also, the bacterial collagenase-resistant peptide from the amino terminus of prepro alpha 1(I) had an apparent molecular weight which was 10 000 greater than the peptide from pro alpha 1(I).

authors

• Prockop, Darwin

published proceedings

• Eur J Biochem

author list (cited authors)

• Graves, P. N., Olsen, B. R., Fietzek, P. P., Prockop, D. J., & Monson, J. M.

citation count

• 23

complete list of authors

• Graves, PN||Olsen, BR||Fietzek, PP||Prockop, DJ||Monson, JM

publication date

• August 1981

publisher

• Wiley  Publisher

published in

• European Journal of Biochemistry  Journal

keywords

• Amino Acid Sequence
• Animals
• Cartilage
• Chick Embryo
• Collagen
• Microbial Collagenase
• Molecular Weight
• Procollagen
• Protein Biosynthesis
• Protein Precursors
• RNA, Messenger
• Rabbits
• Reticulocytes
• Trypsin

PubMed Central ID

• 6269854

Digital Object Identifier (DOI)

• 10.1111/j.1432-1033.1981.tb06411.x

start page

• 363

end page

• 369

volume

• 118

issue

• 2

URL

• http://dx.doi.org/10.1111/j.1432-1033.1981.tb06411.x