CAJ | 학술논문

通过对人发角蛋白的碳、氮稳定同位素分析，揭示个体死亡前短期内的食物结构，我国迄今为止尚无任何报道。在观察新疆罗布淖尔古墓沟墓地M5人发组织结构的基础上，采用两种方法提取了人发角蛋白，并对该个体发与骨的δ13C和δ15N值进行了比较分析。研究结果显示，该个体的发组织结构保存较好；尽管酸处理会导致角蛋白C、N含量明显降低，但对其碳、氮稳定同位素比值影响不大；发角蛋白的δ13C值和δ15N值分别为-18.8‰和14.8‰，表明该个体在约250 d内摄取了大量的动物蛋白。与骨胶原的δ13C值(-18.3‰)和δ15N值(15.5‰)相比，发与骨的碳、氮稳定同位素比值非常相近，结合考古资料，可以看出该个体的食物来源一直较为稳定，源自发达的畜牧业。此外，发与骨之间δ13C和δ15N的细微差异，可能与高蛋白含量的食物在转化为体内胶原蛋白和角蛋白过程中发与骨之间碳、氮同位素的分馏效应较小有关。
통과대인발각단백적탄、담은정동위소분석，게시개체사망전단기내적식물결구，아국흘금위지상무임하보도。재관찰신강라포뇨이고묘구묘지M5인발조직결구적기출상，채용량충방법제취료인발각단백，병대해개체발여골적δ13C화δ15N치진행료비교분석。연구결과현시，해개체적발조직결구보존교호；진관산처리회도치각단백C、N함량명현강저，단대기탄、담은정동위소비치영향불대；발각단백적δ13C치화δ15N치분별위-18.8‰화14.8‰，표명해개체재약250 d내섭취료대량적동물단백。여골효원적δ13C치(-18.3‰)화δ15N치(15.5‰)상비，발여골적탄、담은정동위소비치비상상근，결합고고자료，가이간출해개체적식물래원일직교위은정，원자발체적축목업。차외，발여골지간δ13C화δ15N적세미차이，가능여고단백함량적식물재전화위체내효원단백화각단백과정중발여골지간탄、담동위소적분류효응교소유관。
In contrast to bone collagen, the isotopic composition of the hair keratin is representative of food eaten during the period shortly before demise. Currently, the diet revealed by hair keratin has not yet been reported in China. On the basis of the microstructure of ancient hair from M5 of Gumugou cemetery in Luobunor, Xinjiang, we used two methods to extract keratin from hair and compared theδ13C andδ15N of hair keratin with that of bone collagen from the same individual. The results showed that the organizational structure of ancient hair was well preserved. Although C, N contents decrease during the process of the acid treatment, the δ13C and δ15N of hair keratin were not obviously affected. Theδ13C (?18.8‰) andδ15N (14.8‰) of keratin indicated that the individual consumed much animal protein in about 250 days before death. There were no significant isotopic differences between theδ13C (?18.3‰) andδ15N (15.5‰) of collagen and that of keratin, coupled with the archaeological data, which suggested that the diet of this individual in origin of developed animal husbandry did not vary distinctly in his whole life. In addition, the slightly different δ13C and δ15N between bone collagen and hair keratin were possibly connected to little C, N isotopic fractionation during the transformation from high protein food to collagen and keratin.