Bindings of Ovomucin to Newcastle Disease Virus and Anti-Ovomucin Antibodies and Its Heat Stability Based on Binding Abilities
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- 作者：Yoji Tsuge ; Makoto Shimoyamada ; and Kenji Watanabe
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：1997
- 出版时间：December 1997
- 年：1997
- 卷：45
- 期：12
- 页码：4629 - 4634
- 全文大小：137K
- 年卷期：v.45,no.12(December 1997)
- ISSN：1520-5118
文摘
The bindings of ovomucin, its chemically modified compounds, includingits disulfide-reduced andalkylated 
- and 
-subunits, and desialylated ovomucin to NDV andanti-ovomucin antibodies weredetermined by ELISA. We found that the NeuAc residue in the-subunit greatly contributed tothe binding of ovomucin to NDV, and disulfide bonds in ovomucincontributed to the binding ofovomucin to antibodies. The conformational, biological, andchemical alterations of ovomucin heatedat 60-100 
C for 10 min under the various pH conditions (pH 6-12)were examined on the changesin the ability to NDV and anti-ovomucin antibodies which were alsodetermined by ELISA, alongwith determinations of SDS-PAGE patterns and CD spectra.Ovomucin degraded together withthe increases in temperature and pH, depending on destruction of NeuAcin -subunit, and cleavagesof disulfide bonds in inter- and intrasubunits and peptide bonds in- and -subunits.Keywords: Ovomucin; newcastle disease virus; anti-ovomucin antibodies; heattreatment
- and -subunits, and desialylated ovomucin to NDV andanti-ovomucin antibodies weredetermined by ELISA. We found that the NeuAc residue in the-subunit greatly contributed tothe binding of ovomucin to NDV, and disulfide bonds in ovomucincontributed to the binding ofovomucin to antibodies. The conformational, biological, andchemical alterations of ovomucin heatedat 60-100 C for 10 min under the various pH conditions (pH 6-12)were examined on the changesin the ability to NDV and anti-ovomucin antibodies which were alsodetermined by ELISA, alongwith determinations of SDS-PAGE patterns and CD spectra.Ovomucin degraded together withthe increases in temperature and pH, depending on destruction of NeuAcin -subunit, and cleavagesof disulfide bonds in inter- and intrasubunits and peptide bonds in- and -subunits.Keywords: Ovomucin; newcastle disease virus; anti-ovomucin antibodies; heattreatment