Further observations on the glycoproteins in human ovarian cyst fluids

J.R. Dunstone , W.T.J. Morgan
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引用次数: 31

Abstract

An examination has been made of a number of ovarian cyst fluid glycoproteins that are sparingly soluble water but are similar in general composition to the readily soluble blood-group specific glycloproteins obtained from the same source. Ultracentrifugal analysis of approx. 0.1% w/v solutions of the sparingly soluble materials indicate that they have much larger sedimentation coefficients (S20,w) and molecular weights than have the water-soluble glycoproteins. The sparingly soluble substances have more total amino acids and proportionally more aspartic and glutamic acids and cystine and less serine and threonine than have the soluble glycoproteins. The sparingly soluble substances mostly dissolve in buffered (pH 6.8–7.0, 0.05 M) solutions of thioglycolate, sulphite or cysteine, reagents that bring about the scission of -S-S-bonds. The behaviour and properties of the sparingly soluble glycoproteins suggest that they arise through the building up of relatively small glycoproteins to larger macromolecules through the formation of -S-S- intermolecular associations. A number of ways whereby the formation of these sparingly soluble glycoproteins could occur are discussed.

人卵巢囊肿液中糖蛋白的进一步观察
对一些卵巢囊肿液糖蛋白进行了检查,这些糖蛋白是少量可溶的水,但在一般组成上与从同一来源获得的易溶的血型特异性糖蛋白相似。超离心分析。在0.1% w/v的低溶性溶液中,它们比水溶性糖蛋白具有更大的沉降系数(S20,w)和分子量。与可溶性糖蛋白相比,难溶性物质具有更多的总氨基酸和比例更多的天冬氨酸、谷氨酸和胱氨酸,而较少的丝氨酸和苏氨酸。难溶性物质大多溶解于硫代糖酸盐、亚硫酸盐或半胱氨酸的缓冲溶液(pH 6.8-7.0, 0.05 M)中,这些试剂会导致- s - s键的断裂。少量可溶性糖蛋白的行为和性质表明,它们是通过形成- s - s -分子间结合,将相对较小的糖蛋白构建成较大的大分子而产生的。本文讨论了这些极少溶解的糖蛋白形成的多种途径。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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