A study on the conversion of procollagen: release and recovery of procollagen peptides in the culture medium

B. F. Pontz, P. K. Muller, W. N. Meigel

Publikation: Beitrag in FachzeitschriftArtikelBegutachtung

39 Zitate (Scopus)

Abstract

An in vitro study of the conversion of procollagen to collagen was carried out by culturing embryonic chicken calvaria and labeling them with [3,4 3H]proline and [35S]cysteine. A pulse experiment in the presence of α,α' dipyridyl, an iron chelator, was used to accumulate procollagen in the tissue. The presence of procollagen was demonstrated by the incorporation of [35S]cysteine and by its chromatographic behavior on CM cellulose under denaturing conditions. Using a parallel sample for a subsequent chase experiment in the absence of α,α' dipyridyl, only traces of procollagen were found in the tissue, since [35S]cysteine had disappeared and radioactive material chromatographed with the authentic α chains of lathyritic rat skin collagen. It is proposed that the conversion of procollagen to collagen is paralleled by the release of procollagen peptides into the culture medium, indicating a single step enzymatic cleavage. These peptides were isolated from the culture medium, and their molecular weights were determined as 18,000 for a [35S]cysteine containing and 12,000 for a [35S]cysteine free peptide. Both values are within the size range expected for peptides cleaved from procollagen chains of molecular weights between 110,000 and 120,000.

OriginalspracheEnglisch
Seiten (von - bis)7558-7564
Seitenumfang7
FachzeitschriftJournal of Biological Chemistry
Jahrgang248
Ausgabenummer21
PublikationsstatusVeröffentlicht - 1973
Extern publiziertJa

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