The hatching process in fish embryos : V. Characterization of the hatching protease (chorionase) from the perivitelline fluid of the rainbow trout,Salmo gairdneri rich, as a metalloenzyme.
{"title":"The hatching process in fish embryos : V. Characterization of the hatching protease (chorionase) from the perivitelline fluid of the rainbow trout,Salmo gairdneri rich, as a metalloenzyme.","authors":"Hans E Hagenmaier","doi":"10.1007/BF00574299","DOIUrl":null,"url":null,"abstract":"<p><p>The effects of a number of inhibiting agents on the isolated hatching enzyme of the trout,Salmo gairdneri, have been studied. The enzyme differs from the family of proteases and esterases with serine at the active site, as no inhibition was observed in the presence of PMSF, TPCK, and TLCK. Inhibition is feasible by a number of chelating and ion-metal complexing agents. The results of the inhibition studies indicate that the enzyme belongs to the group of metalloproteases, in contrast to the hatching enzymes of the amphibians and certain moths.</p>","PeriodicalId":54406,"journal":{"name":"Wilhelm Roux Archiv Fur Entwicklungsmechanik Der Organismen","volume":"175 2","pages":"157-162"},"PeriodicalIF":0.0000,"publicationDate":"1974-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF00574299","citationCount":"43","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Wilhelm Roux Archiv Fur Entwicklungsmechanik Der Organismen","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/BF00574299","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 43
Abstract
The effects of a number of inhibiting agents on the isolated hatching enzyme of the trout,Salmo gairdneri, have been studied. The enzyme differs from the family of proteases and esterases with serine at the active site, as no inhibition was observed in the presence of PMSF, TPCK, and TLCK. Inhibition is feasible by a number of chelating and ion-metal complexing agents. The results of the inhibition studies indicate that the enzyme belongs to the group of metalloproteases, in contrast to the hatching enzymes of the amphibians and certain moths.