Abstract
Skin collagen of a female patient with prolidase deficiency was examined for the distribution of borohydride-reducible cross-links and the proportion of type III to type I collagen. Patient's skin contained after reduction more dihydroxylysinonorleucine relative to hydroxylysinonorleucine and type III collagen than expected for normally matured skin. These findings suggest that collagen of the patient's skin failed to follow a time-related normal maturation process and the collagen metabolism was disturbed. The composition of urinary collagen metabolites was also unusual. On the the other hand, her asymptomatic brother with prolidase deficiency showed the normal urinary compositon of collagen matabolites. It is suggested that prolidase deficiency and defect in collagen metabolism independent of it are both responsible for clinical manifestation.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
