Hydroxyproline content and location in relation to collagen thermal stability

✍ Scribed by Tengiz V. Burjanadze

• Publisher: Wiley (John Wiley & Sons)
• Year: 1979
• Tongue: English
• Weight: 348 KB
• Volume: 18
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1979.360180413

✦ Synopsis

A new analysis has been made on studies of the influence of imino acid content on the changes of collagen thermal stability (t,). It is shown that, for the interstitial vertebrate collagens, there is a strict regularity in the changes oft, depending on hydroxyproline content.

No correlation is observed between t , and proline content. Also, no correlation between t , and hydroxyproline content is observed for invertebrate and basement membrane collagens.

On the basis of the reported data, the dependence oft, on hydroxyproline content is considered to he not a correlation between t, and the total content of hydroxyproline, hut only as the correlation between t, and the content of hydroxyproline occurring a t the third position in the sequence (Gly-RZ-R3),. The results agree with the idea that the influence exerted by proline and hydroxyproline on the stabilization of the triple helix of collagen is different.