MISC

1998年11月

Binding activities of Pronase-treated fragments from egg white ovomucin with anti-ovomucin antibodies and Newcastle disease virus

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
  • K Watanabe
  • ,
  • Y Tsuge
  • ,
  • M Shimoyamada

46
11
開始ページ
4501
終了ページ
4506
記述言語
英語
掲載種別
DOI
10.1021/jf980211b
出版者・発行元
AMER CHEMICAL SOC

The prepared gel-like ovomucin and its beta-subunit were treated with Pronase at various ratios (1/25600-1/6.25) to the sample weight at 37 degrees C for 24 h. The concentration, chemical composition, and SDS-polyacrylamide gel electrophoretic patterns of the obtained soluble fractions and their abilities 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 ratio of 1/800 the fragment with the highest binding activity to the antibodies was obtained, and at a ratio 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-resistant fragment (AMM: 120 kDa) at ratios of 1/12.5-1/6.25 with a binding activity to NDV could then be prepared. From the analysis of the fragments of Pronase-treated beta-subunit, the AMM 120-kDa fragment was demonstrated to be a part of the AMM 220-kDa fragment.

Web of Science ® 被引用回数 : 16

リンク情報
DOI
https://doi.org/10.1021/jf980211b
CiNii Articles
http://ci.nii.ac.jp/naid/80010680248
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000077068800008&DestApp=WOS_CPL