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Investigation of total, free, peptide‐bound, protein‐bound, soluble and insoluble collagen hydroxyproline content in tissues from the arabian camel ( Camelus dromedarius )
Author(s) -
Siddiqi N. J,
Aljafari A. A,
Alhomida A. S
Publication year - 2000
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/1099-0844(200012)18:4<243::aid-cbf878>3.0.co;2-n
Subject(s) - hydroxyproline , chemistry , peptide , kidney , biochemistry , medicine , endocrinology , biology
This study was conducted to determine the concentration of total, free, peptide‐bound, protein‐bound, soluble and insoluble collagen hydroxyproline (Hyp) in tissues from the Arabian camel ( Camelus dromedarius ). Results indicated that there were significant differences in the concentration of total, free, peptide‐bound, protein‐bound, soluble and insoluble collagen Hyp in various tissues ( P < 0·01). Camel kidney showed a significantly high concentration of total, free, peptide‐bound and protein‐bound Hyp and collagen content as compared to other tissues examined ( P < 0·01). Kidney also showed a significantly high concentration of soluble collagen Hyp as compared to other tissues examined ( P < 0·01). However, the concentration of insoluble collagen Hyp was significantly high in liver when compared to other tissues ( P < 0·01). These variations may result from differences in the collagen structure and/or composition in this species. Copyright © 2000 John Wiley & Sons, Ltd.