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表面处理的双醛淀粉的扫描电子显微镜分析

SEM analysis of surface-treated dialdehydestarch.

作者信息

Shimizu T, Tanaka Y, Yamazaki Y, Ueda M, Isa I

出版信息

J Biomed Mater Res. 1986 Feb;20(2):247-59. doi: 10.1002/jbm.820200213.

DOI:10.1002/jbm.820200213
PMID:3957962
Abstract

Surface characteristics of protein-treated dialdehydestarch (DAS), which is utilizable as a gastrointestinal sorbent for the treatment of uremia, are examined by scanning electron microscopy (SEM). Unique wrinkles or continuous depressions were observed on the surface of some albumin-treated DAS particles. An increase in concentration and composition of albumin to DAS produces more particles with this kind of rugged surface. On the other hand, gelatin treatment provided a DAS with somewhat rough surface. As the stoichiometric ratio of gelatin to DAS increases, some fibrous or thin-leaves-like projections became outstanding on the surface. Urea-binding properties of protein-treated DAS are just about the same regardless of the protein concentration or composition. In addition, wrinkles or depressions partly observed on the surface of albumin-treated DAS are of little benefit in terms of effective urea binding. These results mean that inherent physical properties of DAS such as dialdehyde content would be a critical factor in urea-sorption ability, rather than surface characteristic or the presence of protein.

摘要

作为治疗尿毒症的胃肠道吸附剂的蛋白质处理过的二醛淀粉(DAS)的表面特性,通过扫描电子显微镜(SEM)进行了研究。在一些白蛋白处理过的DAS颗粒表面观察到独特的皱纹或连续凹陷。白蛋白与DAS的浓度和组成增加会产生更多具有这种粗糙表面的颗粒。另一方面,明胶处理使DAS表面略显粗糙。随着明胶与DAS化学计量比的增加,一些纤维状或薄叶状突起在表面变得突出。无论蛋白质浓度或组成如何,蛋白质处理过的DAS的尿素结合特性大致相同。此外,在白蛋白处理过的DAS表面部分观察到的皱纹或凹陷对有效结合尿素几乎没有益处。这些结果意味着,DAS的固有物理性质如二醛含量将是尿素吸附能力的关键因素,而不是表面特性或蛋白质的存在。

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