Procollagen α2 mRNA is significantly different from procollagen α1(I) mRNA in size or secondary structure

Paul Tolstoshev, Roberta Haber, Ronald Crystal

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The fractionation of fetal calf tendon messenger RNA in 85 percent formamide sucrose gradients shows a separation of the mRNAs coding for pro α1(I) and pro α2 chains of type I collagen. This difference in sedimentation in denaturing gradients suggests that pro α2 mRNA is approxmately 1000 bases shorter than pro α1(I) mRNA. However, such a size difference is significantly greater than would be predicted from consideration of the size of the polypeptide chains coded for by these mRNAs, and thus, residual secondary structure in the mRNAs may contribute to these apparent size differences.

Original languageEnglish
Pages (from-to)818-826
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume87
Issue number3
DOIs
Publication statusPublished - 13 Apr 1979
Externally publishedYes

Fingerprint

Procollagen
Messenger RNA
Tendons
Fractionation
Collagen Type I
Sedimentation
Sucrose
Peptides

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Procollagen α2 mRNA is significantly different from procollagen α1(I) mRNA in size or secondary structure. / Tolstoshev, Paul; Haber, Roberta; Crystal, Ronald.

In: Biochemical and Biophysical Research Communications, Vol. 87, No. 3, 13.04.1979, p. 818-826.

Research output: Contribution to journalArticle

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