Site of hydrolysis of collagen by hot trichloroacetic acid

Jerold A Last, Jay Baer, Christopher Millson

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

When calfskin collagen is treated with trichloroaceti c acid at 90°C, it is hydrolyzed to a mixture of pep-tides, some of which are quite small. Cleavage of collagen by acid seems to occur at bonds between pro-line (or hydroxyproline) and other amino acids, with only a limited specificity for which amino acid donates its amino group to the susceptible peptide bond.

Original languageEnglish (US)
Pages (from-to)149-153
Number of pages5
JournalConnective Tissue Research
Volume4
Issue number3
DOIs
StatePublished - 1976
Externally publishedYes

Fingerprint

Trichloroacetic Acid
Hydrolysis
Collagen
Amino Acids
Acids
Hydroxyproline
Tides
Peptides

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology
  • Orthopedics and Sports Medicine
  • Rheumatology
  • Immunology
  • Nephrology

Cite this

Site of hydrolysis of collagen by hot trichloroacetic acid. / Last, Jerold A; Baer, Jay; Millson, Christopher.

In: Connective Tissue Research, Vol. 4, No. 3, 1976, p. 149-153.

Research output: Contribution to journalArticle

Last, Jerold A ; Baer, Jay ; Millson, Christopher. / Site of hydrolysis of collagen by hot trichloroacetic acid. In: Connective Tissue Research. 1976 ; Vol. 4, No. 3. pp. 149-153.
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