Abstract
Summary
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 NaB 3H4 reduction, there are three intermolecular cross-links; namely, dihydroxylysin-onorleucine, 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. Dihy-droxylysinonorleucine is the principal reduced cross-link in uterine collagen of guinea pig, pig, and cow. Alkaline hydrolysis reveals that dehydrodihydroxylysinonor-leucine and dehydrohydroxylysinonorleucine occur in vivo as glycosylated derivatives.
The authors gratefully acknowledge the supplying of sample materials by Dr. Amy Huang, Fairfax Hospital, Falls Church, Virginia, and Dr. Chien Wei Lan, St. Elizabeths Hospital, Washington, D.C.
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