The plasma membrane H+-ATPases from fungi and yeasts have similar catalytic and molecular properties. A structural comparison has been performed using immunoblot analysis with polyclonal antibodies directed toward the 102 kDa polypeptide of the plasma membrane H+-ATPase from Neurospora crassa. A strong cross-reactivity is observed between the fungal H+-ATPase and the enzyme from the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Structural homologies are indicated also by the analysis of the cross-reactive peptides originated by proteolytic digestion of Neurospora and S.cerevisiae purified enzymes. Neither enzyme from these two sources appears to be glycosylated by a highly sensitive concanavalin A affinity assay on blotted proteins. A glycoprotein of Mr 115000 and pI 4.8-5, which comigrates with a cell cycle-modulated protein on 2D gel, is present in partially purified preparations of plasma membrane H+-ATPase of S.cerevisiae and it is shown to be structurally unrelated to H+-ATPase.
|Titolo:||IMMUNOLOGICAL CROSS-REACTIVITY OF FUNGAL AND YEAST PLASMA-MEMBRANE H-+-ATPASE|
POPOLO, LAURA MARIA (Secondo)
|Parole Chiave:||2D gel electrophoresis; H+-ATPase; Immunoblotting; Peptide mapping|
|Settore Scientifico Disciplinare:||Settore BIO/11 - Biologia Molecolare|
|Data di pubblicazione:||1986|
|Digital Object Identifier (DOI):||10.1016/0014-5793(86)81355-2|
|Appare nelle tipologie:||01 - Articolo su periodico|