The intermolecular cross-links in uterine collagens of guinea pig, pig, cow, and human beings.
The intermolecular cross-links have been studied in the uterine insoluble collagen of guinea pig, pig, cow, and human beings with a single given procedure. After NaB3H4 reduction, there are three intermolecular cross-links; namely, dihydroxylysinonorleucine, hydroxylysinonorleucine, and histidinohydroxymerodesmosine. In human uterine collagen samples these reduced cross-links are present in equal amounts. The reduced intermolecular collagen cross-links of uterine leiomyoma are very similar to those of the normal uterine tissue. Dihydroxylysinonorleucine is the principal reduced cross-link in uterine collagen of guinea pig, pig, and cow. Alkaline hydrolysis reveals that dehydrodihydroxylysinonorleucine and dehydrohydroxylysinonorleucine occur in vivo as glycosylated derivatives.
D000328:Adult; D000367:Age Factors; D000368:Aged; D000818:Animals; D002417:Cattle; D003094:Collagen; D005260:Female; D006168:Guinea Pigs; D006801:Humans; D007889:Leiomyoma / Q000032:analysis; D008875:Middle Aged; D011487:Protein Conformation; D013045:Species Specificity; D013552:Swine; D014594:Uterine Neoplasms / Q000032:analysis; D014599:Uterus / Q000032:analysis*
D003094:Collagen