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Biochemistry Laboratory, Central Leather Research Institute, Adyar, Madras 600 020, India
The effect of protein malnutrition on gingival and uterine collagen cross-linking was studied in female albino rats. The gingival and uterine samples were taken on the 28th day of the experimental period in both groups; the percent reversibility of neutral salt-soluble collagen, and the susceptibility of insoluble collagen to denaturing agents (to KSCN, urea, or pronase) were increased in gingival and uterine samples of protein-deficient animals. The analysis of gingival and uterine samples showed
1 and
2 subunits of neutral salt-soluble collagen appreciably increased, but ß11 and ß12 chains and the aldehyde content were significantly decreased in protein-deficient animals compared to controls. The results indicate that in protein deficiency the cross-linking and maturation of collagen are impaired.
KEY WORDS: protein malnutrition gel reversibility collagen cross-linking maturation process
1 Present address: Department of Surgery, Medical College of Virginis, Virginia Commonwealth University. MCV Station, Richmond, VA 23298.
2 Present address: Division of Metabolism, Department of Pediatrics, Kinderspital, CH-8032, Zurich, Switzerland.
Manuscript received 4 April 1983.