Iamskov I A, Vinogradov A A, Danilenko A N, Maslova L A, Rybakova E Iu, Iamskova V P
Nesmeyanov Institute of Organoelemental Compounds of the Russian Academy of Sciences, Moscow, 117813 Russia.
Prikl Biokhim Mikrobiol. 2001 Jan-Feb;37(1):36-42.
Amino acid composition, structure, and physicochemical properties of a low-molecular-weight glycoprotein from cattle blood serum (SGP) were studied. The content of carbohydrates (represented by mannose-rich oligosaccharides) amounted to 45-50 wt %. The value of specific partial heat of SGP, measured by differential scanning calorimetry (DSC), equaled 1.8 J/g.K, which is characteristic of unfolded proteins. Circular dichroic (CD) spectra of SGP led us to conclude that it is not highly structured and that it occurs in the shape of a statistical globule. The protein was deglycated using anhydrous trifluoromethane sulfonate (TFMS), after which its amino acid composition and the sequence of a fragment were determined. The results indicate that SGP is a protein not studied previously.
对牛血清中的一种低分子量糖蛋白(SGP)的氨基酸组成、结构和物理化学性质进行了研究。碳水化合物(以富含甘露糖的寡糖表示)含量为45 - 50 wt%。通过差示扫描量热法(DSC)测得的SGP比定容热容值为1.8 J/g.K,这是未折叠蛋白质的特征。SGP的圆二色(CD)光谱使我们得出结论,它的结构不紧密,呈统计球状。使用无水三氟甲磺酸酯(TFMS)对该蛋白进行去糖基化处理,之后测定了其氨基酸组成和一个片段的序列。结果表明SGP是一种此前未被研究过的蛋白质。