title: Isolation of rat liver spectrin and identification of functional domains.
abstract: Immunohistochemical studies carried out with liver sections show that spectrin is uniformly distributed along the whole plasma membrane of hepatocytes. The bilecanalicular spectrin is released during the purification of liver subplasma membrane fractions, whereas most of the basolateral spectrin remains tightly bound to the membrane. Spectrin associated with the basolateral membranes has been purified and its subunits isolated. The alpha-subunit retains the ability to bind both calmodulin and actin. Fragments have been obtained either by chemical or by proteolytical digestion of the 240 kDa alpha-subunit. Treatment with CNBr yields fragments of about 30 kDa which bind actin and calmodulin. Digestion with Staphylococcus aureus V-8 proteinase yields a calmodulin-binding fragment of 27 kDa and an actin-binding fragment of 31 kDa.
authors.affiliation: Laboratory of Biochemistry, Swiss Federal Institute of Technology (ETH), Zurich, Switzerland.
authors.forename: R
authors.initials: R
authors.lastname: Falchetto
authors.forename: S
authors.initials: S
authors.lastname: Leutenegger
authors.forename: O
authors.initials: O
authors.lastname: Bachs
authors.forename: J
authors.initials: J
authors.lastname: Serratosa
authors.forename: Y
authors.initials: Y
authors.lastname: Bloemhard
authors.forename: P
authors.initials: P
authors.lastname: Gazzotti
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D002147:Calmodulin / Q000378:metabolism; D002462:Cell Membrane / Q000032:analysis; D003488:Cyanogen Bromide; D005260:Female; D008099:Liver / Q000032:analysis*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000378:metabolism; D051381:Rats; D012697:Serine Endopeptidases; D013049:Spectrin / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D000199:Actins; D002147:Calmodulin; D010446:Peptide Fragments; D013049:Spectrin; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D003488:Cyanogen Bromide