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- W2000778866 abstract "It was reported that on denaturation ovalbumin loses to a considerable extent the ability to react with antibodies against native ovalbumin [ 1,2]. Although many investigators tried to isolate peptides with antigenicity from ovalbumin by enzymic and chemical degradations, there was not any evidence of production of fragments with immunoreactivity [3,4]. These facts imply that the conformation of ovalbumin is responsible to its antigenicity. It is known that native ovalbumin is not digested with trypsin or chymotrypsin at all, owing to the rigid conformation of ovalbumin in native state [4]. In [5], the significance of tyrosine residues in ovalbumin was pointed out as a specific amino acid responsible for antigenic determinants by chemical modification study. We demonstrate here a novel approach for rendering ovalbumin susceptible to hydrolysis with trypsin and were able to obtain two peptides with immunoreactivity. Peptides B and A thus obtained were single polypeptides stretching from N-terminal AcGlyl to Lys 189 with Mr 23 000 and from L.eu 135 to C-terminal Pro,,, containing polysaccharide with Mr 34 000. Both peptides had an ability to bind with anti-ovalbumin serum." @default.
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- W2000778866 date "1982-05-17" @default.
- W2000778866 modified "2023-10-16" @default.
- W2000778866 title "Isolation of peptides with immunoreactivity from OV albumin by trypsin digestion" @default.
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- W2000778866 doi "https://doi.org/10.1016/0014-5793(82)80053-7" @default.
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