Fig. 1 gives the molecular weight distribution for FG1. The weight average molecular weights for the three fish gelatins are given in Table 4. The SEC-MALLS experiments revealed that the fish gelatin, as expected, contained components with different molecular weights. It has previously been found for mammalian gelatins that the broad molecular weight distribution is probably due to the production process, which can give single α-chains, two α-chains covalently cross-linked to give β-chains, and three covalently cross-linked α-chains named γ-chains ([Veis, 1964]). These three types of chains have been identified by electrophoresis and chromatography both for mammalian and fish gelatins ( [Gómez-Guillén et al., 2002 and Norland, 1990]), and the weight average molecular weight of one α-chain was reported to be between 95 and 100 kDa ( [Norland, 1990, Piez, 1968 and Veis, 1964]). The molecular weight of one α-chain can be predicted from the fact that one αα-chain consists of approximately 1000 amino acid residues with an average molecular weight of 110 g/mole, giving a molecular weight of approximately 110 kDa for one α-chain ( [Veis, 1964 and Ward and Courts, 1977]).
參考答案:图一给出了FG1的分子量分布情况。这三种鱼胶的重均分子量在表四中给出。SEC-MALLS实验显示，这些鱼胶如预期的那样，含有不同分子量的组分。以前已经被发现，哺乳动物的明胶具有很宽泛的分子量分布，可能是由于生产过程中，可能产生单α-链；两个α链共价交叉联结产生β-链；以及三个α链共价联结生成γ-链 [Veis, 1964]（这是参考文献，要到最后的参考文献列表依作者和年份寻找）。哺乳动物和鱼明胶里的这三种链已经用电泳、色谱的方法进行辨识[Gómez-Guillén et al., 2002 and Norland, 1990]。并且α-链的重均分子量已经被报道介于95和100kDa之间[Norland, 1990, Piez, 1968 and Veis, 1964]。单个α-链的分子量可以用下面的事实得到预计：单个αα-链是由大约1000个每个平均分子量110（克/摩尔）的氨基酸碎片组成的。这样可以给出每个α-链的分子量大约是110kDa。[Veis, 1964 and Ward and Courts, 1977]
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