| Literature DB >> 11234402 |
I A Iamskov1, A A Vinogradov, A N Danilenko, L A Maslova, E Iu Rybakova, V P Iamskova.
Abstract
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.Entities:
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Year: 2001 PMID: 11234402
Source DB: PubMed Journal: Prikl Biokhim Mikrobiol ISSN: 0555-1099