A lead conversion method for staining thiamine pyrophosphatase and other phosphatases in rat brain after thin layer polyacrylamide gel isoelectric focusing.
P Mazzarello, M Poloni, C Patrini, D Bosone, G Rindi
{"title":"A lead conversion method for staining thiamine pyrophosphatase and other phosphatases in rat brain after thin layer polyacrylamide gel isoelectric focusing.","authors":"P Mazzarello, M Poloni, C Patrini, D Bosone, G Rindi","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Rat brain thiamine pyrophosphatase (TPPase) was separated by thin layer polyacrylamide gel isoelectric focusing (IF) and stained with a modification of the lead conversion method of Allen and Hyncik (1963). 10 bands with TPPase activity were observed in the pH range 4.6-7.1. The overall IF pattern of TPPase was similar to that of uridine diphosphatase and inosine diphosphatase but was clearly different from that of adenosine diphosphatase, p-nitrophenyl phosphatase, alpha-naphthyl phosphatase and thiamine monophosphatase. A semiquantitative assessment of TPPase isoenzymes has been performed using laser densitometry.</p>","PeriodicalId":8726,"journal":{"name":"Basic and applied histochemistry","volume":"32 4","pages":"495-500"},"PeriodicalIF":0.0000,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Basic and applied histochemistry","FirstCategoryId":"1085","ListUrlMain":"","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
Rat brain thiamine pyrophosphatase (TPPase) was separated by thin layer polyacrylamide gel isoelectric focusing (IF) and stained with a modification of the lead conversion method of Allen and Hyncik (1963). 10 bands with TPPase activity were observed in the pH range 4.6-7.1. The overall IF pattern of TPPase was similar to that of uridine diphosphatase and inosine diphosphatase but was clearly different from that of adenosine diphosphatase, p-nitrophenyl phosphatase, alpha-naphthyl phosphatase and thiamine monophosphatase. A semiquantitative assessment of TPPase isoenzymes has been performed using laser densitometry.