Biochemical Characterization of the Mouse Seminal Vesicles Autoantigen (SVA)

碩士 === 國立臺灣大學 === 生化科學研究所 === 82 === Mouse seminal vesicle autotigen (SVA) has been identified recently from our laborary. It is a 19 kDa glycoprotein and the primary structure of tis protein core has been established by cDNA cloning and proyein sequening...

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Main Authors: Luo Ching-wei, 羅清維
Other Authors: Chen Yee-Hsiung
Format: Others
Language:zh-TW
Published: 1994
Online Access:http://ndltd.ncl.edu.tw/handle/80056083017870657226
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spelling ndltd-TW-082NTU001030112016-07-18T04:09:53Z http://ndltd.ncl.edu.tw/handle/80056083017870657226 Biochemical Characterization of the Mouse Seminal Vesicles Autoantigen (SVA) 小白鼠儲精囊自體抗原生化性質的研究 Luo Ching-wei 羅清維 碩士 國立臺灣大學 生化科學研究所 82 Mouse seminal vesicle autotigen (SVA) has been identified recently from our laborary. It is a 19 kDa glycoprotein and the primary structure of tis protein core has been established by cDNA cloning and proyein sequening. The main task fo this work is to study the structure and the function of SVA. The protein was estimated to contain 25 % beta-structure and no helical structure on the basis of its CD. The complex formation of SVA and zinc ion caused no change in the protein conformation. The carbohydrate moeity of SVA composed of galactose, (L)-fucose, mannose,glucose,N-acetylglucosamine,NGNA, NANA. The results of lectin-glycoprotein agglutination test suggested galactose,(L)- fucose as terminal residues of the conjugated carbohydrate. SVA wae not detectable with antiserum angainst phosphoserine, phosphothreonine ,phosphotyrosine ,nor was phosphorylated by protein kinase C and endogeneouskinase. This revealed that SVA is not a phosphoprotein.The results of immunolocation and Western blotting showed that SVA could bind specifically on the midpiece of sperm. Chen Yee-Hsiung 陳義雄 1994 學位論文 ; thesis 65 zh-TW
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description 碩士 === 國立臺灣大學 === 生化科學研究所 === 82 === Mouse seminal vesicle autotigen (SVA) has been identified recently from our laborary. It is a 19 kDa glycoprotein and the primary structure of tis protein core has been established by cDNA cloning and proyein sequening. The main task fo this work is to study the structure and the function of SVA. The protein was estimated to contain 25 % beta-structure and no helical structure on the basis of its CD. The complex formation of SVA and zinc ion caused no change in the protein conformation. The carbohydrate moeity of SVA composed of galactose, (L)-fucose, mannose,glucose,N-acetylglucosamine,NGNA, NANA. The results of lectin-glycoprotein agglutination test suggested galactose,(L)- fucose as terminal residues of the conjugated carbohydrate. SVA wae not detectable with antiserum angainst phosphoserine, phosphothreonine ,phosphotyrosine ,nor was phosphorylated by protein kinase C and endogeneouskinase. This revealed that SVA is not a phosphoprotein.The results of immunolocation and Western blotting showed that SVA could bind specifically on the midpiece of sperm.
author2 Chen Yee-Hsiung
author_facet Chen Yee-Hsiung
Luo Ching-wei
羅清維
author Luo Ching-wei
羅清維
spellingShingle Luo Ching-wei
羅清維
Biochemical Characterization of the Mouse Seminal Vesicles Autoantigen (SVA)
author_sort Luo Ching-wei
title Biochemical Characterization of the Mouse Seminal Vesicles Autoantigen (SVA)
title_short Biochemical Characterization of the Mouse Seminal Vesicles Autoantigen (SVA)
title_full Biochemical Characterization of the Mouse Seminal Vesicles Autoantigen (SVA)
title_fullStr Biochemical Characterization of the Mouse Seminal Vesicles Autoantigen (SVA)
title_full_unstemmed Biochemical Characterization of the Mouse Seminal Vesicles Autoantigen (SVA)
title_sort biochemical characterization of the mouse seminal vesicles autoantigen (sva)
publishDate 1994
url http://ndltd.ncl.edu.tw/handle/80056083017870657226
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