Renaturation and ordering by electron microscopy of the cyanogen bromide peptides from the α2 chain of chick skin collagen

Shogo Igarashi, Andrew Kang, Jerome Gross

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The three larger CNBr peptides from the α2 chain of chick skin collagen, α2-CB3, α2-CB4, α2-CB5 and a peptide with a molecular weight of about 60,000 containing an uncleaved methionyl residue, α2-CB(3-5), were separately renatured and aggregated into SLS crystallites for electron microscopy. Comparison of the resultant cross-striation patterns with those of the renatured α2 chains plus previously determined positions of two of the three smaller peptides by chemical means indicates the order of the CNBr peptides to be α2-CB(1-0-4-2-3-5). This coincides with that determined by chemical and isotope labelling techniques described in an accompanying paper.

Original languageEnglish (US)
Pages (from-to)697-702
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume38
Issue number4
DOIs
StatePublished - Feb 20 1970

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Cyanogen Bromide
Electron microscopy
Electron Microscopy
Skin
Collagen
Peptides
Isotope Labeling
Crystallites
Isotopes
Labeling
Molecular Weight
Molecular weight

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Renaturation and ordering by electron microscopy of the cyanogen bromide peptides from the α2 chain of chick skin collagen. / Igarashi, Shogo; Kang, Andrew; Gross, Jerome.

In: Biochemical and Biophysical Research Communications, Vol. 38, No. 4, 20.02.1970, p. 697-702.

Research output: Contribution to journalArticle

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