Abstract
The 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 the 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.
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Yamskov, I.A., Vinogradov, A.A., Danilenko, A.N. et al. Low-Molecular-Weight Glycoprotein from Cattle Blood Serum: Structure and Properties. Applied Biochemistry and Microbiology 37, 29–35 (2001). https://doi.org/10.1023/A:1002884106796
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DOI: https://doi.org/10.1023/A:1002884106796