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  1. 掲載誌一覧
  2. Memoirs of the Faculty of Agriculture, Kagoshima University
  3. vol.7(1)
  1. 農学部
  2. 農学部・紀要論文

Comparative Chemical Studies on the Proteins in the Quail and Chicken Egg Whites (I) Electrophoresis, CM-cellulose chromatography and gradient extraction with salt on the whole white

http://hdl.handle.net/10232/9479
http://hdl.handle.net/10232/9479
ed4bb97a-088f-455f-9cd6-0709b3cb5b22
名前 / ファイル ライセンス アクション
AA00732376_v7n1_p15-33.pdf AA00732376_v7n1_p15-33.pdf (4.5 MB)
Item type 紀要論文 / Departmental Bulletin Paper(1)
公開日 2012-05-01
タイトル
タイトル Comparative Chemical Studies on the Proteins in the Quail and Chicken Egg Whites (I) Electrophoresis, CM-cellulose chromatography and gradient extraction with salt on the whole white
タイトル言語 en
著者 KOGA, Katsuya

× KOGA, Katsuya

WEKO 98473

en KOGA, Katsuya

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言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ departmental bulletin paper
アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
要約
内容記述タイプ Other
内容記述 1) The pH value, specific conductance, the combined sugar-protein ratio and the nitrogen content of the Japanese quail egg white are larger than each corresponding value of the chicken egg white. Nitrogen content in the dry matter was especially high, coming to 17.5 %. However, specific gravity was rather small.
2) The quail and chicken egg whites were separated together into three components with the carbonate buffer electrophoretically and each mobility of the three components in the quail egg white is slightly smaller than that of the chicken. The former was separated into four components at pH 7.80, μ 0.144, though the latter was separated into six components and both egg whites revealed respectively the patterns resembling those just above-mentioned, at pH 7.00, μ 0.11.
Under the condition of pH 4.40, μ 0.11, six components were observed respectively in both egg whites, differing with each other in their separated patterns. Even at such condition, both negatively charged and no charged components were observed in the quail, though negatively charged component, only, in the chicken. In the electrophoresis at pH 7.80 and 4.40, the mobilities of each component in the quail egg white were smaller than those of the corresponding components in the chicken egg white.
3) The elution diagrams of egg white proteins of the two species separated by CM-cellulose revealed eight components respectively, resembling in their separated patterns one another. Comparing with the pH value of the eluate at each peak of the chicken egg white proteins, only the quail ovomucoid is low, while on the other hand, ovalbumin, globulins and conalbumin are slightly high and lysozyme equals one another. The protein being anionic at pH 4.0 (Component A) and ovomucoid are more in the quail than in the chicken, while the components corresponding to ovalbumin and lysozyme in the former appeared less in quantity. When the component A in the quail and chicken egg whites was examined spectrophotometrically, the former showed the absorption maximum at 280 mμ, the latter, at 265 mμ. Component A appeared to be only one band on the gel electrophoresis.
4) Six components were ascertained respectively in the quail and chicken egg white proteins by the gradient extraction with ammonium sulfate. The sugar content of the protein which was not precipitated by full saturation of ammonium sulfate was larger in the former, coming to 37 %, and 23 % in the latter. Comparing with the chicken proteins the component corresponding to ovalbumin and conalbumin in the quail egg white is small in quantity. Except for component B, the sugar-protein ratios of all components were slightly larger in the quail than in the chicken.
5) Quail ovalbumin was ascertained to differ markedly from the chicken one electrophoretically. The former was separated into two components, the latter, only one, in both carbonate and phoshate buffers. The mobility of the main component of the quail ovalbumin was smaller than that of the chicken ovalbumin. At pH 5.20, the quail ovalbumin was separated into three components, in which only one was positively charged, while the chicken ovalbumin revealed only one component. At pH 4.80 the former was separated into three components and the latter revealed two components what are called ovalbumin A_1, and A_2, and the mobility of the main component of the quail
ovalbumin was smaller than that of the chicken one. The quail albumin revealed three components and the chicken albumin, only one, under the condition of pH 4.60, where the major component in the former was left unrunning, and the component of the latter gave the mobility amounting to -0.36 x 10^-5. The sugar contents in the quail and chicken ovalbumins were ascertained to be 4.32 % and 2.70 % respectively. Neutral sugar of the quail ovalbumin was fixed to be mannose and galactose, agreeing with the chicken one.
内容記述言語 en
収録雑誌名 en : Memoirs of the Faculty of Agriculture, Kagoshima University

巻 7, 号 1, p. 15-33, 発行日 1969-03-25
作成日
日付 1969-03-25
日付タイプ Issued
ISSN
収録物識別子タイプ PISSN
ISSN 04530853
NII書誌ID(雑誌)
収録物識別子タイプ NCID
NC ID AA00732376
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
NDC
主題Scheme NDC
主題 646
公開者・出版者
出版者 鹿児島大学
出版者言語 ja
公開者・出版者
出版者 Kagoshima University
出版者言語 en
関連(relation)(relationType設定なし)
識別子タイプ URI
関連識別子 http://hdl.handle.net/10232/9478
備考
備考言語 en
備考 Has errata: http://hdl.handle.net/10232/9478
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