Ovalbumin subfractionation and individual difference in ovalbumin microheterogeneity.
نویسندگان
چکیده
منابع مشابه
Glycopeptide from Ovalbumin
1. The structure of the carbohydrate component of the glycopeptide isolated from the proteolytic digest of ovalbumin has been investigated by chemical and enzymic methods. 2. The results are consistent with the presence of a single carbohydrate prosthetic group, linked through its reducing end group to the peptide chain. 3. Further, all the 2-amino-2-deoxy-D-glucose units appear to be in the N-...
متن کاملStructural differences of ovalbumin and S-ovalbumin revealed by denaturing conditions.
We found, by circular dichroism and Raman spectroscopy measurements, that the secondary structure of the native ovalbumin and of its heat-stable form, called S-ovalbumin, is a probe of the structural differences between the two proteins. Small angle X-ray scattering and circular dichroism measurements performed on the two proteins under denaturing conditions, with different concentrations of gu...
متن کاملSoluble Ovalbumin In Vivo Cross-Presented Much More Efficiently than Cell-Associated Ovalbumin Is
متن کامل
Structures of the Carbohydrate Moiety of Ovalbumin Glycopeptide III and the Difference in Specificity
Endo-P-N-acetylglucosaminidase C,, hydrolyzes 75% of ovalbumin glycopeptide III, while endo+N-acetylglucosaminidase H cleaves it completely. For the purpose of clarifying the difference of substrate specificities of C,, and H enzymes, the structures of the oligosaccharides released from the glycopeptide by these enzymes were studied. The oligosaccharides released by C,, enzyme were Mancul + 6 (...
متن کاملConformational changes involved in the switch from ovalbumin to S-ovalbumin.
For the first time a comparative study on conformational differences between native ovalbumin and its heat-stable form, called S-ovalbumin, using small angle x-ray scattering, is reported. To detect a different pathway in the folding mechanism of the two proteins, scattering measurements have been performed on ovalbumin and S-ovalbumin denatured with different concentrations of guanidine hydroc...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)69252-5