Binding Activities of Pronase-Treated Fragments from Egg White Ovomucin with Anti-ovomucin Antibodies and Newcastle Disease Virus
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- 作者：Kenji Watanabe ; Yoji Tsuge ; and Makoto Shimoyamada
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：1998
- 出版时间：November 1998
- 年：1998
- 卷：46
- 期：11
- 页码：4501 - 4506
- 全文大小：111K
- 年卷期：v.46,no.11(November 1998)
- ISSN：1520-5118
文摘
The prepared gel-like ovomucin and its 
-subunit were treated with Pronase at various ratios (1/25600-1/6.25) to the sample weight at 37 
C for 24 h. The concentration, chemical composition,and SDS-polyacrylamide gel electrophoretic patterns of the obtained soluble fractions and theirabilities to bind to anti-ovomucin antibodies and Newcastle disease virus (NDV) were measured.At a ratio of 1/6400 the highest soluble fraction (solubility: nearly 100%) was obtained. At a ratioof 1/800 the fragment with the highest binding activity to the antibodies was obtained, and at aratio of 1/50 the fragments with the disulfide bonds intact (apparent molecular masses, AMMs: 55,45, and 40 kDa) which showed binding to the antibodies were prepared and partially characterized.Fragments (AMMs: 220, 120, and 100 kDa) at ratios of 1/3200-1/800 and the final Pronase-resistantfragment (AMM: 120 kDa) at ratios of 1/12.5-1/6.25 with a binding activity to NDV could then beprepared. From the analysis of the fragments of Pronase-treated -subunit, the AMM 120-kDafragment was demonstrated to be a part of the AMM 220-kDa fragment.Keywords: Ovomucin; anti-ovomucin antibodies; Newcastle disease virus; Pronase treatment
-subunit were treated with Pronase at various ratios (1/25600-1/6.25) to the sample weight at 37 C for 24 h. The concentration, chemical composition,and SDS-polyacrylamide gel electrophoretic patterns of the obtained soluble fractions and theirabilities to bind to anti-ovomucin antibodies and Newcastle disease virus (NDV) were measured.At a ratio of 1/6400 the highest soluble fraction (solubility: nearly 100%) was obtained. At a ratioof 1/800 the fragment with the highest binding activity to the antibodies was obtained, and at aratio of 1/50 the fragments with the disulfide bonds intact (apparent molecular masses, AMMs: 55,45, and 40 kDa) which showed binding to the antibodies were prepared and partially characterized.Fragments (AMMs: 220, 120, and 100 kDa) at ratios of 1/3200-1/800 and the final Pronase-resistantfragment (AMM: 120 kDa) at ratios of 1/12.5-1/6.25 with a binding activity to NDV could then beprepared. From the analysis of the fragments of Pronase-treated -subunit, the AMM 120-kDafragment was demonstrated to be a part of the AMM 220-kDa fragment.Keywords: Ovomucin; anti-ovomucin antibodies; Newcastle disease virus; Pronase treatment