Yuji Hirano, A. Kobayashi, Akira Haruki, H. Haga, M. Hara, Toyoji Sato, T. Ōhashi, K. Sasagawa, T. Miura, Yukio Shima, S. Watanabe
{"title":"Characterization of serum alkaline phosphatase separated at or near the origin in polyacrylamide gel using detergents, antibodies and neuraminidase","authors":"Yuji Hirano, A. Kobayashi, Akira Haruki, H. Haga, M. Hara, Toyoji Sato, T. Ōhashi, K. Sasagawa, T. Miura, Yukio Shima, S. Watanabe","doi":"10.2198/JELECTROPH.52.25","DOIUrl":null,"url":null,"abstract":"We studied serum samples which showed alkaline phosphatase (ALP) activity at or near the origin of the polyacrylamide gel electrophoresis. 1) Sucrose monolaurate (final concentration, 1.7%) treatment produced a new ALP band (SM-ALP band). 2) The SM-ALP band disappeared from the original region with anti-human placental ALP antibody and appeared at the high molecular region. 3) ALP activity of SM-ALP band was completely inactivated by heat treatment (at 65°C for 10 min). 4) The molecular mass was estimated to be approximately 350 kDa by a 5-20% (linear gradient) polyacrylamide slab gel electrophoresis. We concluded that the SM-ALP band was intestinal ALP tetramer.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"90 1","pages":"25-27"},"PeriodicalIF":0.0000,"publicationDate":"2008-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of capillary electrophoresis","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2198/JELECTROPH.52.25","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
We studied serum samples which showed alkaline phosphatase (ALP) activity at or near the origin of the polyacrylamide gel electrophoresis. 1) Sucrose monolaurate (final concentration, 1.7%) treatment produced a new ALP band (SM-ALP band). 2) The SM-ALP band disappeared from the original region with anti-human placental ALP antibody and appeared at the high molecular region. 3) ALP activity of SM-ALP band was completely inactivated by heat treatment (at 65°C for 10 min). 4) The molecular mass was estimated to be approximately 350 kDa by a 5-20% (linear gradient) polyacrylamide slab gel electrophoresis. We concluded that the SM-ALP band was intestinal ALP tetramer.