Rao J S, Rao V H, Bose S M
J Nutr. 1983 Aug;113(8):1459-63. doi: 10.1093/jn/113.8.1459.
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 alpha 1 and alpha 2 subunits of neutral salt-soluble collagen appreciably increased, but beta 11 and beta 12 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.
在雌性白化大鼠中研究了蛋白质营养不良对牙龈和子宫胶原交联的影响。两组均在实验期的第28天采集牙龈和子宫样本;蛋白质缺乏动物的牙龈和子宫样本中,中性盐溶性胶原的可逆百分比以及不溶性胶原对变性剂(硫氰酸钾、尿素或链霉蛋白酶)的敏感性增加。牙龈和子宫样本分析显示,与对照组相比,蛋白质缺乏动物中性盐溶性胶原的α1和α2亚基明显增加,但β11和β12链以及醛含量显著降低。结果表明,在蛋白质缺乏时,胶原的交联和成熟受到损害。