Institut for Biomedicin

Mikael Esmann

Occlusion of Rb+ after extensive tryptic digestion of shark rectal gland Na,K-ATPase

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

  • Institut for Fysiologi og Biofysik
  • Molekylærbiologisk Institut
Na,K-ATPase from rectal glands of Squalus acanthias has been subjected to proteolysis with trypsin. The E1- and E2-forms of the enzyme can be distinguished from the inactivation patterns at low trypsin concentrations, as previously seen with kidney enzyme. Extensive degradation by trypsin in the presence of 5 mM Rb+ yields membrane fragments with a 19 kDa peptide as the major proteolytic fragment of the alpha-subunit. The sequence of the N-terminal 40 residues of this peptide is almost identical to that of a similar proteolytic fragment isolated by Capasso et al. (Capasso, J.M., Hoving, S., Tal, D.M., Goldshleger, R. and Karlish, S.J.D. (1992) J. Biol. Chem. 267, 1150-1158) using kidney Na,K-ATPase. Rb+ occlusion can be fully retained under these circumstances, supporting the findings with kidney enzyme that only minor parts of the alpha-subunit are required to form a functional occlusion-site.
OriginalsprogEngelsk
TidsskriftBBA General Subjects
Vol/bind1108
Nummer2
Sider (fra-til)247-252
Antal sider6
ISSN0304-4165
StatusUdgivet - 27 jul. 1992

Se relationer på Aarhus Universitet Citationsformater

ID: 36021352