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.
IMMUNOLOGICAL CROSS-REACTIVITY OF FUNGAL AND YEAST PLASMA-MEMBRANE H-+-ATPASE / M. VAI, L. POPOLO, L. ALBERGHINA. - In: FEBS LETTERS. - ISSN 0014-5793. - 206:1(1986), pp. 135-141.
Titolo: | IMMUNOLOGICAL CROSS-REACTIVITY OF FUNGAL AND YEAST PLASMA-MEMBRANE H-+-ATPASE | |
Autori: | 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 | |
Rivista: | ||
Tipologia: | Article (author) | |
Digital Object Identifier (DOI): | http://dx.doi.org/10.1016/0014-5793(86)81355-2 | |
Appare nelle tipologie: | 01 - Articolo su periodico |