The effect of age on amino acid composition of human skin collagen

J Gerontol. 1978 Jul;33(4):498-503. doi: 10.1093/geronj/33.4.498.

Abstract

To study the effect of age on amino acid composition of human skin collagen, skins from 8 women aged 0 to 93 were extracted with acetone and EDTA and then gelatinized. Gelatin was purified by extraction with chloroform-methanol and DEAE cellulose chromatography. Hydroxyproline was spectrophotometrically determined and its contents were essentially the same (12.6%). Amino acid analysis indicated no significant age-related variations in the contents of proline, hydroxyproline, lysine, and hydroxylysine over the range of 0 to 93 years of age. The content of cysteine was reasonably low (0.4 to 0.6 per 1,000 amino acid residues) except in the cases of those 0 and 93 years of age. Aldehyde content was slightly lower in young cases than in infant and old cases. These results indicate that the changes in cross-links derived from aldehyde may be responsible for the effect of age.

MeSH terms

  • Adult
  • Age Factors
  • Aged
  • Aging*
  • Aldehydes / analysis
  • Amino Acids / analysis*
  • Child
  • Collagen / analysis*
  • Cysteine / analysis
  • Female
  • Humans
  • Hydroxylysine / analysis
  • Hydroxyproline / analysis
  • Infant, Newborn
  • Lysine / analysis
  • Middle Aged
  • Proline / analysis
  • Skin / analysis*

Substances

  • Aldehydes
  • Amino Acids
  • Hydroxylysine
  • Collagen
  • Proline
  • Lysine
  • Cysteine
  • Hydroxyproline